Agrochemical adhesion synergist based on plant-derived protein, and preparation method therefor and use thereof

Abstract

The present application relates to the field of agrochemical adjuvants, and relates to an agrochemical protein adhesion synergist based on a plant-derived protein, and a preparation method therefor and a use thereof. Said synergist comprises the following raw materials in parts by weight: 20-500 parts of a plant-derived protein, 50-450 parts of a protein dispersant, and 20-350 parts of a protein stabilization and protection agent. The product of the present application improves the utilization rate of agrochemicals and reduces problems such as grain yield reduction and environmental pollution caused by the loss of agrochemicals. Moreover, as the protein degrades into amino acids, plant growth can be promoted, and the resistance of plants to abiotic stress is improved, thereby reducing dosage of agrochemicals while enhancing efficacy of agrochemicals.

Description

Plant source protein-based adhesion enhancer for agricultural chemicals and preparation method and application thereof

[0001] Cross-reference to related applications

[0002] The present application claims priority to the Chinese patent application No. 202411572189.1, filed on November 5, 2024, with the title of "Plant source protein-based adhesion enhancer for agricultural chemicals and preparation method and application thereof", the whole content of which is incorporated herein by reference. TECHNICAL FIELD

[0003] The present application relates to the technical field of pesticide adjuvants, in particular to a plant source protein-based adhesion enhancer for agricultural chemicals and preparation method and application thereof. BACKGROUND

[0004] The information disclosed in this Background section is only for the purpose of increasing the understanding of the general background of the present application and should not be taken as an acknowledgement or any form of suggestion that this information forms prior art with regard to the present application.

[0005] It is crucial to ensure food security by firmly promoting the reduction of fertilizers and pesticides and increasing their efficiency. Agricultural chemicals (such as pesticides, fertilizers, and biological stimulants) are important agricultural production materials, which are essential for preventing diseases and pests and promoting stable grain production. However, due to the super-hydrophobic / hydrophobic properties of plant leaf surfaces and insect body surfaces, agricultural chemicals lack adhesion to plant leaf surfaces and insect body surfaces, which results in bouncing or splashing during spraying, leading to the loss of more than half of the agricultural chemicals. Even if a part of the agricultural chemicals remains on the plant leaf or insect body surface, it will be washed away by rain, ultimately resulting in less than 0.1% of the sprayed pesticides playing a role. The part of the agricultural chemicals lost due to rainwater washing will enter the soil, pollute groundwater, and harm the ecosystem. The problem of overuse of agricultural chemicals due to low utilization rate has attracted widespread attention.

[0006] To improve the utilization rate of pesticides and fertilizers, the commonly used method is to add organic silicon surfactants to pesticides and fertilizers. These surfactants are difficult to degrade, not friendly to plants and the environment, and may cause secondary environmental pollution.

[0007] Therefore, there is an urgent need for a safe and environmentally friendly, low-cost, easily degradable, and rain-resistant pesticide adjuvant. SUMMARY

[0008] OBJECTIVE

[0009] The purpose of this application is to provide a plant-derived protein-based agricultural chemical protein adhesion enhancer, its preparation method, and its application. The agricultural chemical protein adhesion enhancer of this application is safe and environmentally friendly, inexpensive, easily degradable, resistant to rain washout, and significantly enhances the efficacy of pesticides and fertilizers. It can respond to the national call to promote the reduction and efficiency of pesticides and fertilizers, promote high and stable grain yields, and at the same time avoid environmental pollution.

[0010] Solution

[0011] To achieve the purpose of this application, in a first aspect, this application provides an agrochemical protein adhesion enhancer based on plant-derived protein, comprising the following raw materials in the following weight ratios: 20-500 parts of plant-derived protein, 50-450 parts of protein dispersant, and 20-350 parts of protein stabilizer.

[0012] Further, the raw materials include the following parts by weight: 20-500 parts of plant-derived protein, 50-450 parts of protein dispersant, and 20-350 parts of protein stabilizer.

[0013] Optionally, the raw materials include the following parts by weight: 200-500 parts of plant-derived protein, 50-200 parts of protein dispersant, and 25-100 parts of protein stabilizer.

[0014] Optionally, the raw materials include the following parts by weight: 200-500 parts of plant-derived protein, 50-120 parts of protein dispersant, and 25-80 parts of protein stabilizer.

[0015] Optionally, the raw materials include the following proportions by weight: 300-500 parts of plant-derived protein, 50-120 parts of protein dispersant, and 25-50 parts of protein stabilizer.

[0016] Optionally, the plant-derived protein can spontaneously aggregate at the interface to form a film.

[0017] Furthermore, the protein dispersant is selected from one or more of the following: polyether sulfonate, chain carboxylate polymer, carboxylate polymer, alkoxy fatty alcohol phosphate, polycarboxylate, sodium lignosulfonate, phosphate ester, alkyl naphthalene sulfonate formaldehyde condensate, naphthalene sulfonate, formaldehyde condensate, long-chain fatty alcohol polyoxyethylene ether, alkylphenol polyoxyethylene ether, fatty acid polyoxyethylene ester, polyoxyethylene alkylamine, glycerol fatty acid ester, sorbitan fatty acid ester, dehydrated sorbitan fatty acid ester, sucrose fatty acid ester, sodium alginate, carboxymethyl cellulose, carboxyethyl cellulose, acrylic polymer, polyvinylpyrrolidone, polyacrylamide, anionic surfactant, and nonionic surfactant.

[0018] And / or, the protein stabilizer is selected from one or more of ethylene glycol, isopropanol, diethyl ether, propylene oxide, toluene, xylene, methyl acetate, ethyl acetate, propyl acetate, pentane, hexane, octane, cyclohexane, cyclohexanone, methylcyclohexanone, chlorobenzene, dichlorobenzene, dichloromethane, acetone, methyl butyl ketone, methyl isobutyl ketone, etc., ethylene glycol monomethyl ether, ethylene glycol monoethyl ether, ethylene glycol monobutyl ether, acetonitrile, pyridine, phenol, pectin, xanthan gum, and other plant / microbial polysaccharides.

[0019] Furthermore, the plant-derived protein is selected from any one or more proteins contained in the plants listed in the table below:

[0020] Furthermore, the plant-derived protein is selected from one or more of the following plant proteins: legume protein, grass protein, jujube protein, rose family protein, madder family protein, convolvulaceae family protein, linseed protein, solanaceae family protein, asteraceae family protein, cruciferous family protein, bryophyte family protein, cucurbitaceae family protein, moraceae family protein, purslane family protein, theaceae family protein, sesamoides family protein, gentianaceae family protein, soapberry family protein, sapotaceae family protein, pinaceae family protein, nymphaeaceae family protein, anabolicae family protein, sedge family protein, urticaceae family protein, ginger family protein, ginkgoaceae family protein, cypress family protein, olive family protein, peony family protein, ephedrine family protein, violaceae family protein, dioscoreaceae family protein, brassica family protein, and ospermaceae family protein.

[0021] Optionally, legume proteins include one or more of the following: soybean protein, peanut protein, mung bean protein, kidney bean protein, black bean protein, pea protein, red bean protein, broad bean protein, and alfalfa protein; optionally, grass protein includes one or more of the following: corn protein, oat protein, barley protein, wheat protein, rye protein, buckwheat protein, rice protein, and millet protein; optionally, Osmunda species protein includes bracken protein; optionally, Rosaceae species protein includes one or more of the following: almond protein and papaya protein; optionally, Malvaceae species protein includes one or more of the following: cottonseed protein and okra protein. Optionally, the protein from Convolvulaceae plants includes one or more of purple sweet potato protein and sweet potato protein; Optionally, the protein from Dioscoreaceae plants includes sweet potato protein; Optionally, the protein from Cruciferae plants includes one or more of broccoli protein and rapeseed protein; Optionally, the protein from Cucurbitaceae plants includes one or more of pumpkin protein, cucumber seed protein, pumpkin seed protein, bitter melon protein, and gourd protein; Optionally, the protein from Sapindaceae plants includes one or more of lychee protein and longan / dried longan protein; Optionally, the protein from Nymphaeaceae plants includes lotus seed protein; Optionally, the protein from Bryophyllaceae plants includes water shield protein; Optionally, The proteins from plants in the Urticaceae family include one or more of nettle protein and mulberry leaf protein; optionally, the proteins from the Juglandaceae family include walnut protein; optionally, the proteins from the Linaceae family include flaxseed protein; optionally, the proteins from the Solanaceae family include potato protein; optionally, the proteins from the Asteraceae family include sunflower seed protein; optionally, the proteins from the Bryaceae family include bryophyte protein; optionally, the proteins from the Moraceae family include hemp seed protein; optionally, the proteins from the Portulacaceae family include purslane protein; optionally, the proteins from the Theaceae family include tea protein; optionally, the proteins from the Pseudoaceae family include sesame protein; optionally, the proteins from the Gentianaceae family include gentian protein. White; Optionally, the plant protein from the Sapotaceae family includes avocado protein; Optionally, the plant protein from the Pinaceae family includes pine nut protein; Optionally, the plant protein from the Anacardiaceae family includes cashew nut protein; Optionally, the plant protein from the Cyperaceae family includes sedge protein; Optionally, the plant protein from the Zingiberaceae family includes ginger protein; Optionally, the plant protein from the Ephedra family includes ephedra protein; Optionally, the plant protein from the Ginkgoaceae family includes ginkgo protein; Optionally, the plant protein from the Cupressaceae family includes cypress fruit protein; Optionally, the plant protein from the Burseraceae family includes olive protein; Optionally, the plant protein from the Violaceae family includes violet protein; Optionally, the plant protein from the Paeoniaceae family includes peony protein and rose protein;

[0022] Optionally, it also includes water, in a content of 200 to 800 parts by weight, or optionally 600 to 800 parts by weight.

[0023] Furthermore, one or more of the plant-derived proteins undergo physical and chemical modification;

[0024] Optionally, physical modification includes one or more of the following: pH adjustment, salt concentration, heat treatment, ultrasonic treatment, microwave treatment, high pressure treatment, radio frequency treatment, and mechanical stirring.

[0025] Optionally, chemical modification includes initiating monomer polymerization containing functional groups from the protein, or grafting functional polymers or small molecules onto the protein surface; optionally, the initiating functional groups include one or more of carboxyl, hydroxyl, carbonyl, and amino groups; optionally, the functional polymers used to initiate functional polymerization or grafting include one or more of polyethylene glycol, polyacrylic acid, polylactic acid, and polysaccharides; optionally, the small molecules used to initiate functional polymerization or grafting include polyphenols, polycarboxylic acids, ketones, glycosides, etc. One or more of the following: plant essential oils, nicotine-like substances, and other plant secondary metabolites; optional polysaccharides including one or more of the following: starch, cellulose, algal polysaccharides, chitin / chitosan, plant polysaccharides, microbial polysaccharides, anionic polysaccharides, cationic polysaccharides, and neutral polysaccharides; optional polyphenols including flavonoids such as epicatechin, cyanidin, quercetin, and naringenin; phenolic acids such as gallic acid, caffeic acid, chlorogenic acid, and rhein; stilbene compounds such as resveratrol; stilbene compounds such as jasmonic acid; stilbene compounds such as echinacea extract; and lignans. One or more of the following: tannic acid, etc.; optionally, polycarboxylic acids including one or more of oxalic acid, citric acid, malic acid, glycyrrhizic acid, etc.; optionally, plant essential oils including one or more of tea tree oil, thyme oil, rose oil; chemical modification also includes the introduction of reducing thiol compounds or protein denaturing agents; optionally, reducing thiol compounds including one or more of mercaptoethanol, cysteine, glutathione, mercaptosuccinic acid, dihydrolipoic acid, tris(2-carboxyethyl)phosphohydrochloride; protein denaturing agents including urea, salts The chemical modification includes one or more of guanidine acid, guanidine isothiocyanate, sodium dodecyl sulfate, and arginine; the chemical modification also includes enzymatic cross-linking or degradation, wherein the cross-linking enzymes include one or more of transglutaminase, oxidases (tyrosinase, laccase, peroxidase, thiol oxidase), lipoxygenase, and gamma-glutamyl endopeptidase; the oxidases include one or more of tyrosinase, laccase, peroxidase, and thiol oxidase; and the degrading enzymes include one or more of papain, bromelain, and soybean protease.

[0026] In a second aspect, an agricultural chemical formulation is provided, comprising agricultural chemicals and the agricultural chemical protein adhesion enhancer described in the first aspect; optionally, the agricultural chemicals include one or more of pesticides, fertilizers, and biostimulants.

[0027] Furthermore, pesticides include one or more of the following: insecticides, fungicides, antiviral agents, herbicides, acaricides, nematicides, rodenticides, plant growth regulators, insect growth regulators, plant immune inducers, fumigants, biological pesticides, mineral-derived pesticides, organic synthetic pesticides, and seed dressing agents.

[0028] And / or, fertilizers include one or more of the following: organic fertilizers, chemical fertilizers, compound fertilizers, slow-release fertilizers, bio-fertilizers, micronutrient fertilizers, foliar fertilizers, soil conditioners, and organic-inorganic compound fertilizers.

[0029] And / or, biostimulants include one or more of the following: humic acid substances, seaweed extracts, free amino acids, complex organic matter, non-organic minerals, microorganisms and their secondary metabolites, plant extracts and their secondary metabolites, chitin and chitosan derivatives, beneficial chemical elements, and antitranspirants.

[0030] Optionally, the target surface of the agrochemical can be any one of the following: the surface of an insect body, plant leaves, plant roots and stems, or seed surface.

[0031] Optionally, the concentration of the agricultural chemical protein adhesion enhancer is 5–20 mL / 10 L, or optionally 10 mL / 10 L.

[0032] Thirdly, a method for preparing the agrochemical protein adhesion enhancer described in the first aspect, or the agrochemical formulation described in the second aspect, is provided, comprising the following steps:

[0033] 1) First, add the plant-derived protein to 200-800 parts of deionized water, then add the protein dispersant and disperse and mix.

[0034] 2) Add the protein stabilizer to the protein mixture obtained in step 1), and homogenize it by shearing and sand milling to obtain a stable plant-derived protein adhesive; optionally, stable plant-derived protein adhesives of different grades from 3nm to 60nm can be obtained.

[0035] It may also include: 3) In the implementation, a certain number of agricultural chemicals are mixed with water or an aqueous solution containing protein stabilizers, and then the plant-derived protein adhesive obtained in step 2) is added. Depending on the application scenario, the product is diluted 200 to 2000 times and applied to the target surface by spraying, sprinkling, smearing, dipping, spinning or sputtering to increase the retention of agricultural chemicals.

[0036] Fourthly, this invention provides an application of plant-derived protein in the preparation of protein adhesion synergists for agricultural chemicals, wherein the plant-derived protein is selected from one or more of the following plant proteins: legume protein, grass protein, jujube protein, rose family protein, madder family protein, convolvulaceae family protein, linseed protein, solanaceae family protein, asteraceae family protein, cruciferous family protein, bryophyte family protein, cucurbitaceae family protein, moraceae family protein, purslane family protein, theaceae family protein, sesamoides family protein, gentianaceae family protein, soapberry family protein, sapotaceae family protein, pinaceae family protein, nymphaeaceae family protein, anabolicae family protein, sedge family protein, urticaria family protein, ginger family protein, ginkgoaceae family protein, cypress family protein, olive family protein, peony family protein, ephedrine family protein, violaceae family protein, dioscoreaceae family protein, brassica family protein, and ospermaceae family protein.

[0037] The common feature of the proteins contained in these plants is that they can spontaneously aggregate at the interface to form a film, making them universally applicable and non-antagonistic in agricultural production. Beneficial effects

[0038] The product of this application improves the utilization rate of agricultural chemicals, reduces problems such as reduced grain yield and environmental pollution caused by the loss of agricultural chemicals, and as proteins degrade into amino acids, it can promote plant growth, improve the plant's resistance to abiotic stress, and achieve the goal of reducing the amount of agricultural chemicals and increasing efficiency.

[0039] The protein product of this application is easy to use; after mixing, it can be sprayed, spread, dipped, spin-coated, or sputtered onto the target surface.

[0040] The preparation method of the product in this application is simple, the main component is plant-derived protein, it has high biocompatibility, is environmentally friendly, and safe for animals and plants.

[0041] In this application, the protein products are characterized by their wide availability, low price, environmental friendliness, and resistance to rain washout, providing a solid technical foundation for promoting the reduction of chemical fertilizers and pesticides and accelerating the comprehensive green transformation of agriculture. Attached Figure Description

[0042] One or more embodiments are illustrated by way of example with reference to the accompanying drawings, and these illustrative examples are not intended to limit the embodiments. The term "illustrative" as used herein means "serving as an example, embodiment, or illustration." Any embodiment illustrated herein as "illustrative" is not necessarily to be construed as superior to or better than other embodiments.

[0043] Figure 1: A scanning electron microscope image of the protein adhesion enhancer product of Example 1 in Test Example 1 of this application sprayed on the surface of a blank lotus leaf.

[0044] Figure 2 shows the surface of a blank lotus leaf (a), the surface of a lotus leaf after spraying with a suspension of the pesticide imidacloprid (70% active ingredient content, deionized water as solvent) (b), and the surface of a lotus leaf after spraying with a mixture of the protein adhesion enhancer product of Example 2 and the imidacloprid suspension (c).

[0045] Figure 3 is a fluorescence microscope image of the protein film formed by spraying the protein adhesion enhancer product of Example 3 and the imidacloprid suspension in Test Example 3 of this application, showing its resistance to rain erosion.

[0046] Figure 4 shows the control effect of the plant-derived protein adhesion enhancer in Example 4 of this application, mixed with agricultural chemicals (fipronil + pyridaben), on whiteflies on peppers.

[0047] Figure 5 shows the control effect of the plant-derived protein adhesion enhancer in Example 5 of this application, mixed with agricultural chemicals (thiamethoxam and spinosad), on cowpea thrips.

[0048] Figure 6 shows the control effect of the plant-derived protein adhesion enhancer in Example 6 of this application, mixed with agricultural chemicals (chlorantraniliprole suspension and indoxacarb), on rice leaf roller.

[0049] Figure 7 shows the control effect of the plant-derived protein adhesion enhancer of Example 7 in Test Example 7 of this application, when mixed with agricultural chemicals (oxadixyl·metalaxyl-M), on grape downy mildew.

[0050] Figure 8 shows the effect of mixing the plant-derived protein adhesion enhancer with agricultural chemicals (including amino acid foliar fertilizer) in Example 8 of this application on the quality improvement and yield increase of cruciferous crop Chinese cabbage.

[0051] Figure 9 shows the effect of mixing the plant-derived protein adhesion enhancer with agricultural chemicals in Example 9 of this application on the quality improvement and yield increase of Dali winter jujube.

[0052] Figure 10 shows the control effect of the plant-derived protein adhesion enhancer of Example 10 of Test Example 10 of this application, when mixed with agricultural chemicals, on the aphid disease of Ruixue apple.

[0053] Figure 11 shows the control effect of the plant-derived protein adhesion enhancer in Example 11 of this application, when mixed with agricultural chemicals, on wheat scab disease.

[0054] Figure 12 is a comparison chart of the synergistic effects of the plant protein synergist product in Example 2 of Test Example 12 of this application and that of animal protein (bovine serum albumin) + reducing agent (TCEP). Detailed Implementation

[0055] To make the objectives, technical solutions, and advantages of the embodiments of this application clearer, the technical solutions in the embodiments of this application will be clearly and completely described below. Obviously, the described embodiments are only some embodiments of this application, not all embodiments. Based on the embodiments in this application, all other embodiments obtained by those skilled in the art without creative effort are within the scope of protection of this application. Unless otherwise expressly stated, throughout the specification and claims, the term "comprising" or its variations such as "including" or "comprising of," etc., will be understood to include the stated elements or components, and does not exclude other elements or other components.

[0056] Furthermore, to better illustrate this application, numerous specific details are provided in the following detailed embodiments. Those skilled in the art should understand that this application can be implemented without certain specific details. In some embodiments, materials, elements, methods, and means well-known to those skilled in the art are not described in detail in order to highlight the main points of this application.

[0057] The raw materials used in this application can be commercially available products or obtained through self-extraction. Self-extraction can be achieved through common plant-derived protein extraction methods such as alkali dissolution and acid precipitation, reverse micelle extraction, enzymatic extraction, organic solvent extraction, salt dissolution extraction, flash extraction, reverse micelle extraction, solvent extraction, enzymatic methods, precipitation, and Osborne fractionation extraction.

[0058] Example 1

[0059] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of soybean protein (purchased from Shanghai Yuanye Biotechnology Co., Ltd.), 100 parts of polyether carboxylate dispersant, 25 parts of ethylene glycol stabilizer, and 800 parts of deionized water.

[0060] Example 2

[0061] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts corn protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 80 parts polyether carboxylate dispersant, 20 parts phosphate dispersant, 25 parts ethyl acetate stabilizer, and 800 parts deionized water.

[0062] Example 3

[0063] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts peanut protein (purchased from Xi'an Lingfeng Biotechnology Co., Ltd.), 40 parts polyether carboxylate dispersant, 40 parts phosphate dispersant, 20 parts naphthalene sulfonate dispersant, 25 parts ethylene glycol monomethyl ether stabilizer, and 800 parts deionized water.

[0064] Example 4

[0065] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of walnut protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 20 parts of fatty acid polyoxyethylene ester dispersant, 20 parts of sucrose fatty acid ester dispersant, 15 parts of sodium alginate dispersant, 25 parts of pyridine stabilizer, 25 parts of pectin stabilizer, and 800 parts of deionized water.

[0066] Example 5

[0067] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts almond protein (purchased from Shaanxi Xiazhou Biotechnology Co., Ltd.), 100 parts walnut protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts cottonseed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts purple sweet potato protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 20 parts long-chain fatty alcohol polyoxyethylene ether dispersant, 20 parts polyoxyethylene alkylamine dispersant, 15 parts sodium alginate dispersant, 10 parts propyl acetate stabilizer, 20 parts pectin stabilizer, 20 parts ethylene glycol monoethyl ether stabilizer, and 800 parts deionized water.

[0068] Example 6

[0069] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts oat protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts mung bean protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts potato protein (purchased from Shaanxi Xiazhou Biotechnology Co., Ltd.), 100 parts flaxseed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 20 parts sodium lignin sulfonate dispersant, 20 parts phosphate ester dispersant, 15 parts sucrose fatty acid ester dispersant, 10 parts methyl acetate stabilizer, 20 parts pectin stabilizer, 20 parts ethylene glycol monoethyl ether stabilizer, and 800 parts deionized water.

[0070] Example 7

[0071] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts papaya protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts kidney bean protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts sweet potato protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts cottonseed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 20 parts sodium lignin sulfonate dispersant, 20 parts phosphate ester dispersant, 15 parts sucrose fatty acid ester dispersant, 10 parts methyl acetate stabilizer, 20 parts pectin stabilizer, 20 parts ethylene glycol monoethyl ether stabilizer, and 800 parts deionized water.

[0072] Example 8

[0073] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts sunflower seed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts black bean protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts sweet potato protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts broccoli protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 20 parts polyether carboxylate dispersant, 20 parts phosphate ester dispersant, 10 parts naphthalene sulfonate dispersant, 50 parts ethylene glycol monomethyl ether stabilizer, and 800 parts deionized water.

[0074] Example 9

[0075] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of pea protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 30 parts of fatty acid polyoxyethylene ester dispersant, 30 parts of sucrose fatty acid ester dispersant, 40 parts of sodium alginate dispersant, 25 parts of pectin stabilizer, and 800 parts of deionized water.

[0076] Example 10

[0077] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of red bean protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 80 parts of polyether carboxylate dispersant, 20 parts of phosphate dispersant, 25 parts of ethyl acetate stabilizer, and 800 parts of deionized water.

[0078] Example 11

[0079] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts broad bean protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts polyether carboxylate dispersant, 25 parts ethylene glycol stabilizer, and 800 parts deionized water.

[0080] Example 12

[0081] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of barley protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 30 parts of fatty acid polyoxyethylene ester dispersant, 30 parts of sucrose fatty acid ester dispersant, 40 parts of sodium alginate dispersant, 25 parts of pectin stabilizer, and 800 parts of deionized water.

[0082] Example 13

[0083] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts wheat protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 40 parts polyether carboxylate dispersant, 40 parts phosphate dispersant, 20 parts naphthalene sulfonate dispersant, 25 parts ethylene glycol monomethyl ether stabilizer, and 800 parts deionized water.

[0084] Example 14

[0085] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts oat protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts polyether carboxylate dispersant, 25 parts ethylene glycol stabilizer, and 800 parts deionized water.

[0086] Example 15

[0087] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of cottonseed protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of polyether carboxylate dispersant, 25 parts of ethylene glycol stabilizer, and 800 parts of deionized water.

[0088] Example 16

[0089] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts almond protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts moss protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts rapeseed protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts pumpkin protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 30 parts sodium lignin sulfonate dispersant, 30 parts phosphate ester dispersant, 60 parts sucrose fatty acid ester dispersant, 10 parts methyl acetate stabilizer, 10 parts pectin stabilizer, 5 parts ethylene glycol monoethyl ether stabilizer, and 800 parts deionized water.

[0090] Example 17

[0091] The protein adhesion enhancer product in this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts of bracken protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts of hemp seed protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of rye protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of cucumber seed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water.

[0092] Example 18

[0093] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts bitter melon protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts pumpkin protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts buckwheat protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts pumpkin seed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 30 parts sodium lignosulfonate dispersant, 30 parts phosphate ester dispersant, 60 parts sucrose fatty acid ester dispersant, 10 parts methyl acetate stabilizer, 10 parts pectin stabilizer, 5 parts ethylene glycol monoethyl ether stabilizer, and 800 parts deionized water.

[0094] Example 19

[0095] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts of purslane protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts of alfalfa protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of cucurbita protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of tea protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts of polyether carboxylate dispersant, 25 parts of ethylene glycol stabilizer, and 800 parts of deionized water.

[0096] Example 20

[0097] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts rice protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts millet protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts gentian protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts sesame protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 40 parts polyether carboxylate dispersant, 40 parts phosphate ester dispersant, 20 parts naphthalene sulfonate dispersant, 25 parts ethylene glycol monomethyl ether stabilizer, and 800 parts deionized water.

[0098] Example 21

[0099] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts of litchi protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts of avocado protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of pine nut protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of okra protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 30 parts of sodium lignosulfonate dispersant, 30 parts of phosphate ester dispersant, 60 parts of sucrose fatty acid ester dispersant, 10 parts of methyl acetate stabilizer, 10 parts of pectin stabilizer, 5 parts of ethylene glycol monoethyl ether stabilizer, and 800 parts of deionized water.

[0100] Example 22

[0101] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts lotus seed protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts cashew nut protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts water shield protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts sedge protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts polyether carboxylate dispersant, 25 parts ethylene glycol stabilizer, and 800 parts deionized water.

[0102] Example 23

[0103] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts alfalfa protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts longan / dried longan protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts nettle protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts mulberry leaf protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts polyether carboxylate dispersant, 25 parts ethylene glycol stabilizer, and 800 parts deionized water.

[0104] Example 24

[0105] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts of rose protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts of ginger protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of ephedrine protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of ginkgo protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 30 parts of sodium lignosulfonate dispersant, 30 parts of phosphate ester dispersant, 60 parts of sucrose fatty acid ester dispersant, 10 parts of methyl acetate stabilizer, 10 parts of pectin stabilizer, 5 parts of ethylene glycol monoethyl ether stabilizer, and 800 parts of deionized water.

[0106] Example 25

[0107] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 100 parts of cypress fruit protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 100 parts of olive protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of violet protein (purchased from Xi'an Jinshuo Fruit Industry Co., Ltd.), 100 parts of peony protein (purchased from Shanxi Hengran Biotechnology Co., Ltd.), 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water.

[0108] Example 26

[0109] The protein adhesion enhancer product of this embodiment is prepared by physical modification of 400 parts of plant protein (adjusting pH=10 and sonicating for 30 minutes), adding 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water, followed by dispersion, shearing, and nano-grinding.

[0110] Example 27

[0111] The protein adhesion enhancer product of this embodiment is prepared by chemically modifying 400 parts of plant protein (grafting functional polymers such as polyethylene glycol, polylactic acid, and polyvinyl alcohol; in this embodiment, polyvinyl alcohol is used to modify the strong hydrophobic glycidol protein of white kidney bean. Reference: Zhang Zifan, Wu Sisi, Liu Chunxiu, et al. Research progress on functional properties and modification of kidney bean protein [J]. Food and Fermentation Industries, 2024, 50(05):357-366.DOI:10.13995 / j.cnki.11-1802 / ts.034670), and then adding 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water through dispersion, shearing, and nano-milling.

[0112] Example 28

[0113] The protein adhesion enhancer product of this embodiment was prepared by dispersing, shearing, and nano-milling 400 parts of plant protein (blended with polysaccharides, polyphenols, polycarboxylic acids, and plant essential oils; in this embodiment, rice protein modified with dextran was used, with a mass ratio of rice protein to dextran of 1:6, a protein concentration of 4.03 mg / mL, and a reaction time of 22 min. At this time, the maximum grafting degree reached 48.1%. Reference: Hua Jingxian. Study on microwave heating grafting coupling reaction of rice protein-dextran [D]. Jiangnan University, 2008.), and then adding 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water.

[0114] Alternatively, a modified material composed of phosphorylated perilla meal protein and chitosan can be used. By means of free radical grafting, polyphenol protocatechuic acid (PA) and chitosan are copolymerized, and a complex of the two is constructed based on hydrogen bonding and electrostatic interaction. Reference: [1] Zhao Qiaoli. Construction, characterization and performance study of perilla meal protein-based high internal phase emulsion system [D]. Jiangnan University, 2023. DOI:10.27169 / d.cnki.gwqgu.2023.000050.

[0115] Example 29

[0116] The protein adhesion enhancer product of this embodiment is made from 400 parts of plant protein through chemical modification (addition of reducing thiol compounds such as cysteine, glutathione, thiosuccinic acid, and dihydrolipoic acid; the chemical modification method can be found in the reference: An Hongzhou, Chen Jinhuan, Yan Hanxiao, et al. Study on the influence of different modification techniques on the functional properties of plant protein [J / OL]. China Oils and Fats, 1-14 [2024-10-13]. https: / / doi.org / 10.19902 / j.cnki.zgyz.1003-7969.240401. This embodiment uses cysteine ​​to modify rice bran protein, and its preparation method is as follows: under a relatively weak alkaline condition (pH=8) and a relatively low temperature (45℃), L-cysteine ​​is used as a reducing agent. The reducing agent was added at a concentration of 0.07% (the ratio of reducing agent to rice bran protein), and the reaction time was 1.5 h. Ultrasonic treatment was used as an adjunct, with a power of 280 W and an ultrasonic time of 8 min. Under these conditions, the rice bran protein extraction rate reached 46.59%, which was 16.62%, 9.35%, and 7.4% higher than that of the alkali method, ultrasonic method, and reducing agent method, respectively. The purity of the rice bran protein reached 82%. (Reference: Sun Xiuting. Ultrasonic-reducing agent extraction and modification process and its functional study of rice bran protein [D]. Fujian Agriculture and Forestry University, 2015.) Then, 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water were added, followed by dispersion, shearing, and nano-grinding to prepare the final product.

[0117] Example 30

[0118] The protein adhesion enhancer product in this embodiment is made by enzymatically decomposing 400 parts of plant protein, and adding transglutaminase, tyrosinase, laccase, peroxidase, thiol oxidase, lipoxygenase, gamma-glutamyl endopeptidase, papain, bromelain, and soy protease, etc. (In this embodiment, papain and bromelain are used to enzymatically hydrolyze soy protein isolate. The optimal process for papain enzymatic hydrolysis of SPI is: hydrolysis time 3h, hydrolysis temperature 60℃, enzyme dosage 0.35g, pH 7.5, substrate concentration 5g / 100mL; bromelain...) The optimal process for enzymatic hydrolysis of SPI is: hydrolysis time 10h, hydrolysis temperature 40℃, enzyme dosage 0.35g, pH 7.5, and substrate concentration 5g / 100mL. References: [1] Chen Yafang. Study on preparation of soybean oligopeptides and their ACE inhibitory activity and chelation characteristics [D]. Chinese Academy of Agricultural Sciences, 2009.), and then add 40 parts of polyether carboxylate dispersant, 40 parts of phosphate dispersant, 20 parts of naphthalene sulfonate dispersant, 25 parts of ethylene glycol monomethyl ether stabilizer, and 800 parts of deionized water to prepare the product by dispersion, shearing, and nano-grinding.

[0119] All the above quantities are in grams (g), but can also be in kilograms (kg), mg, etc.

[0120] This application may also replace the thiamethoxam, imidacloprid, abamectin, flonicamid, etc. in Examples 1-30 with other pesticides, fertilizers, plant growth regulators, biostimulants, etc.; replace the soybean protein, oat protein, almond protein, sweet potato protein, walnut protein, alfalfa protein, rose protein, etc. in Examples 1-30 with other plant-containing proteins; replace the phosphate esters, naphthalene sulfonates, polyether carboxylates, etc. in Examples 1-30 with other dispersants; and replace the ethylene glycol, pectin, ethylene glycol monomethyl ether, ethylene glycol monoethyl ether, etc. in Examples 1-30 with other stabilizers, all of which are within the scope of protection of this application.

[0121] To demonstrate the advantages of plant protein as a pesticide adjuvant, the inventors conducted performance tests on the protein adhesion enhancer products prepared in Examples 1-30, as detailed below:

[0122] Test Example 1. Verification of the film-forming effect of protein adhesion enhancer products

[0123] The target surface was selected as a lotus leaf with superhydrophobic properties. The diluted protein product of Example 1 was evenly sprayed onto the surface of a 5cm×5cm lotus leaf, allowed to air dry naturally, and then the film formation was observed using a scanning electron microscope (see Figure 1). The results showed that the protein adhesion enhancer product of this application can form a uniform, large-area film on the superhydrophobic lotus leaf surface.

[0124] Test Example 2. Verification of the spreading and adhesion ability of protein adhesion enhancer products

[0125] Test Method: A protein adhesion synergist was mixed with 10-100 parts of imidacloprid water-dispersible granules (70% active ingredient content) at a 1:1 volume ratio. The mixture was diluted 10-2000 times and sprayed onto the surface of lotus leaves (superhydrophobic properties) as the product group. A control group was established by spraying only imidacloprid water-dispersible granules (without the protein adhesion synergist, at the same dilution ratio). The spreading and adhesion of the product on the plant leaf surface were observed and recorded by photograph. A specific test was conducted as follows:

[0126] Product group: Mix the diluted imidacloprid solution (70% active ingredient content, diluted 10 times with water) and the diluted protein adhesion enhancer product solution from Example 2 at a volume ratio of 1:1, and spray evenly on the surface of a 5cm×5cm lotus leaf.

[0127] Control group: Only imidacloprid suspension was sprayed (without protein adhesion enhancer, and the same dilution ratio).

[0128] Then, photos were taken to record the results, as shown in Figure 2. The results show that when only imidacloprid suspension was sprayed, the spreading and adhesion area on the lotus leaf surface was small (see Figure 2b), while the protein adhesion enhancer product of this application can enable imidacloprid suspension to spread and adhere over a large area on the superhydrophobic lotus leaf surface (see Figure 2c).

[0129] Test Example 3. Verification of Rainwater Erosion Resistance of Protein Adhesion Enhancer Products

[0130] Test Method: A protein adhesion synergist was mixed with 10-100 parts of imidacloprid water-dispersible granules (70% active ingredient content), diluted 10-2000 times, and high-pressure sprayed onto the surface of lotus leaves as the product group. A control group was established by spraying only imidacloprid water-dispersible granules (without the protein adhesion synergist, at the same dilution ratio). Tap water was used to simulate rainwater washing for 2 minutes. The leaves were marked with fluorescent dye, and the residue of the product on the lotus leaf surface before and after rainwater washing was observed using a fluorescence microscope, and photographs were taken and recorded. A specific test was conducted as follows:

[0131] Product group: Mix the diluted imidacloprid solution (70% active ingredient content, diluted 10 times with water) and the diluted protein adhesion enhancer product solution of Example 3 at a volume ratio of 1:1, spray it on the surface of the superhydrophobic lotus leaf, let it dry, and then rinse it with tap water to simulate rain for 2 minutes.

[0132] Control group: Imidacloprid suspension was sprayed alone on the superhydrophobic surface as a control experiment. After drying, it was rinsed with tap water to simulate rain for 2 minutes.

[0133] Sodium fluorescein was used as a fluorescent labeling dye. The results were captured in a photograph and are shown in Figure 3. The results, when observed under a fluorescence microscope, demonstrate that the protein product of this application has good resistance to rain erosion.

[0134] Test Example 4. Effect of Protein Adhesion Enhancer on Reduced-Dosage and Enhanced Control of Whitefly on Peppers

[0135] This experiment used the protein adhesion synergist product from Example 4, diluted 500-2000 times with 10-100 parts of 15% pyridaben (EC) and 20% dinotefuran (SC), respectively, and then mixed. The experiment was conducted in Dongsun Village, Yanliang District, Xi'an City, Shaanxi Province, to test its reduced-dosage and synergistic effect in the chemical control of whiteflies on peppers. The experiment included three treatment groups and one control group. Each treatment used 10L of water and was applied once via foliar spraying (specific treatment methods are shown in Table 1). Pest mortality was checked on the third day after application, and the mortality rate was recorded seven days after application. The results of Example 4 are shown in Figure 4.

[0136] Table 1 Experimental Treatment

[0137] In Table 1 and Figure 4, 100% represents the initial pesticide application rate, and 75% represents a reduction of the relative initial pesticide application rate to 75%.

[0138] Figure 4 shows that the protein synergist product of Example 4, when mixed with the highly penetrating insecticide dinotefuran, did not cause any phytotoxicity to chili peppers. Seven days after spraying, comparing the number of whiteflies killed in the 100% pesticide group and the "100% + synergist" group, it was found that using the protein synergist product of this application increased pesticide adhesion to vegetable leaves, promoting better efficacy and thus increasing the number of dead whiteflies. Comparing the number of whiteflies killed in the 100% pesticide group and the "75% + synergist" group, it was found that using the protein synergist product of this application reduced the amount of pyridaben pesticide used by 25%.

[0139] It has been verified that the protein synergist products in Examples 5-7 can also reduce the amount of pyridaben pesticide used by at least 25%.

[0140] Therefore, the protein synergist product of this application will not cause phytotoxicity when mixed with the highly penetrating neonicotinoid insecticide fipronil, and it also has a significant dosage reduction and synergistic effect, which can reduce the amount of pyridaben pesticide used by 25%.

[0141] Test Example 5. Effect of Protein Adhesion Enhancer on Reduced-Amount and Enhanced Control of Cowpea Thrips

[0142] The experiment used the protein adhesion synergist product from Example 8. The experiment was conducted at the Guilin Yang Agricultural Vegetable Base in Meilan District, Haikou City, covering an area of ​​approximately 1.5 mu (approximately 0.067 hectares). The soil type was sandy, with a pH of 5.5 and an organic matter content of 11.1 g / kg. The experiment involved a single application of the herbicide during the peak flowering period of cowpeas, using 60 L / mu (specific treatment methods are shown in Table 2). Control efficacy was assessed 3 and 6 days after application. The field control efficacy results of the mixture of the protein adhesion synergist product from Example 8 and the herbicide are shown in Figure 5.

[0143] Table 2 Experimental Treatment

[0144] Figure 5 shows that the addition of the protein synergist from Example 8 to the pesticide enhanced the control of cowpea thrips, reducing pesticide usage by up to 70%. The synergistic effect was most pronounced 3 days after application.

[0145] It has been verified that the protein synergist products of Examples 9-11 can also reduce the amount of pesticides used by at least 30% of thiamethoxam or spinosad.

[0146] The protein synergist product of this application will not cause phytotoxicity when mixed with insecticides such as thiamethoxam and spinosad. Moreover, it has a significant effect of reducing dosage and enhancing efficacy, which can reduce the amount of pesticide used by 25%-30%.

[0147] Test Example 6. A study on the reduced-use and enhanced-efficacy control of rice leaf folder by a protein adhesion synergist product.

[0148] The experiment used the protein adhesion enhancer product from Example 12, and the site was set up at the Zhaofeng planting base in Tanxia Town, Lingchuan County, Guangxi Province. The rice variety was "Deyou 108". The experiment was conducted by applying the pesticide once during the booting stage of rice, with 30 L of water per mu (the specific experimental treatment method is shown in Table 3). The control efficacy of the protein adhesion enhancer product from Example 12 after mixing with the pesticide was statistically analyzed at 3, 7 and 14 days after application (see Figure 6).

[0149] Table 3 Experimental Treatment

[0150] Figure 6 shows that, compared with the efficacy of single-agent pesticides, the addition of the protein synergist from Example 12 significantly enhanced the control efficacy against rice leaf roller. The control efficacy was better with a 30% reduction in pesticide dosage and the addition of the protein synergist compared to the single-agent pesticide group at 100% dosage. The most significant control effect was observed 7 days after application.

[0151] It has been verified that the protein synergist products of Examples 13-15 can also reduce the amount of pesticides used by at least 30% of chlorantraniliprole or indoxacarb.

[0152] The protein synergist product of this application will not cause phytotoxicity when mixed with insecticides such as chlorantraniliprole and indoxacarb, and has a significant effect of reducing dosage and enhancing efficacy, which can reduce the amount of pesticides used by 30%.

[0153] Test Example 7. Trial of Reduced-Dosage Synergistic Effect of Protein Adhesion Enhancer on Grape Downy Mildew Control

[0154] The experiment was conducted at the Xi'an Urban Agriculture Experiment and Demonstration Station in Chang'an District, Xi'an City, using the protein adhesion enhancer product of Example 16. The grape variety was Hutai No. 8, with an 8-year-old tree and a planting size of 2.4m × 1.0m. The grapes were in the fruit enlargement stage and the early stage of downy mildew disease at the time of application. The product was applied three times, with 15L / mu of water used for application (the specific experimental treatment method is shown in Table 4). The control effect was recorded after each application. The control effect of the protein adhesion enhancer product of Example 16 mixed with the agent is shown in Figure 7.

[0155] Table 4 Experimental Treatment

[0156] The results in Figure 7 show that, compared with the efficacy of single-agent pesticides, the addition of protein synergists to pesticides significantly enhanced the control of grape downy mildew; the efficacy of pesticides reduced by 20% and with the addition of protein synergists was better than that of pesticides used at 100% single-agent dosage.

[0157] It has been verified that the protein synergist products of Examples 17-19 can also reduce the amount of pesticide used by at least 20% of oxadixyl·metalaxyl.

[0158] The protein synergist product of this application will not cause phytotoxicity when mixed with oxadixyl-M-methyl-M-methyl. In addition, it has a significant effect of reducing dosage and enhancing efficacy, which can reduce the amount of pesticide used by 20%.

[0159] Test Example 8. Experiment on the effect of protein adhesion synergists on reducing yield, improving quality and increasing production of Chinese cabbage hearts.

[0160] The experiment used the protein adhesion enhancer product from Example 20. The experiment was conducted at the Kangli plantation in Weizhao Village 3, Wangmang Street, Chang'an District, Xi'an City, Shaanxi Province. Two groups were set up, with each group receiving 10 L / mu of fertilizer water, applied once every 15 days for a total of 3 applications (specific experimental treatment methods are shown in Table 5). After harvest, the growth indicators and quality of the rapeseed in each treatment were measured, including stem diameter, stem length, fresh weight, dry weight, water content, chlorophyll content, vitamin content, protein content, and yield per mu. The effect of the protein adhesion enhancer product from Example 20 mixed with amino acid foliar fertilizer is shown in Tables 6 and 7, and Figure 8.

[0161] Table 5 Experimental Treatment

[0162] Table 6. Growth indicators of Chinese cauliflower during the application of protein synergists as foliar fertilizer.

[0163] Table 7. Results of nutrient index determination of Chinese cauliflower during the application of protein synergists as foliar fertilizer.

[0164] Figure 8 shows the experimental results. The chlorophyll content, vitamin C content and protein content of the rapeseed core in the enhanced group of Example 20 were significantly higher than those in the control group. There were fewer pests and diseases, the leaves were more colorful, and the yield increased by 5%. In addition, some rapeseed cores in the enhanced group flowered earlier, which proves that the enhancer has a certain effect on promoting early maturity.

[0165] It has been verified that the protein enhancer products in Examples 21-23 can also improve the quality and yield of rapeseed hearts.

[0166] Therefore, when using foliar fertilizer for rapeseed, the protein synergist product of this application can be reasonably added and used to improve the quality and increase the yield of rapeseed.

[0167] Test Example 9. Effect of Protein Adhesion Enhancer on Reduced-Dosage Synergistic Effect of Dali Jujube

[0168] The experiment used the protein adhesion enhancer product of Example 24 to conduct a pesticide reduction and efficiency enhancement test on Dali winter jujube at the Dali County Fruit Industry Development Center in Weinan City, Shaanxi Province. The experiment consisted of 5 treatments (the specific test methods are shown in Table 8). Each treatment used 60L of water and was applied 5 times. After the fruit was harvested in September, the yield and quality of each treatment were tested, including single fruit weight, fruit shape index, fruit firmness, soluble solids content, and titratable acid content. Pesticide residues were also tested. The effect of the protein adhesion enhancer product of Example 24 mixed with pesticides is shown in Tables 9 and 10 and Figure 9.

[0169] Table 8 Experimental Treatment

[0170] In Table 8, the synergist refers to the protein adhesion synergist of Example 24, which was added at a rate of 10 mL / 10 L of water (i.e., the protein adhesion synergist of Examples 24-26 was diluted 1000 times). 90%, 70%, 50%, and 30% refer to the amount of pesticide added being 90%, 70%, 50%, and 30% of the recommended dosage.

[0171] Table 9. Fruit Shape Index of Dali Winter Jujube

[0172] Table 10 Pesticide Residues in Dali Winter Jujubes

[0173] The results showed that the average single fruit weight of all five treatments (using the protein adhesion enhancer product of Example 24) met the standard for premium-grade fruit with a single fruit weight of over 18g as stipulated in the Shaanxi Provincial Local Standard DB61 "Geographical Indication Product Dali Winter Jujube" published in 2020 (see Figure 9). The single fruit weight of the 50% and 70% reduction groups was significantly higher than that of the control group (CK), increasing by 16.83% and 49.67% respectively (see Figure 9). The soluble solids content of the jujube fruit in the 50% reduction group was significantly higher than that in the control group. The fruit shape index of the control group, the 30% reduction group, and the 50% reduction group was greater than 1, indicating an oblong shape; the fruit shape index of the 70% and 90% reduction groups tended to be 1, indicating a round shape (see Table 9). The pesticide residue level of the 50% reduction group was significantly lower than that of the control group, and the pesticide residue levels of all reduction groups were lower than the maximum allowable residue level (see Table 10). It has been verified that the protein synergist products of Examples 25 and 26 can also increase the weight of a single fruit and reduce pesticide residues while reducing the dosage by 30%, 50%, and 70%, respectively.

[0174] In conclusion, the protein enhancer product of this application can be reasonably added and used to improve the quality of winter jujubes.

[0175] Test Example 10. Trial of Reduced-Dosage and Enhanced Control of Apple Aphid Disease by Protein Adhesion Enhancer Product

[0176] The experiment used the protein adhesion synergist product of Example 27 to conduct a pesticide reduction and efficacy control experiment on the aphid disease of Ruixue apples in Caojia Village, Leiya Town, Baishui County, Weinan City, Shaanxi Province. The experiment consisted of 5 treatments (the specific experimental treatment methods are shown in Table 11). Each treatment used 30L of water and applied the pesticide once. The aphid population was investigated 1, 3, and 7 days after the pesticide was applied, and the control efficacy was calculated. The control efficacy of the protein adhesion synergist product of Example 27 mixed with the pesticide is shown in Figure 10.

[0177] Table 11 Experimental Treatment

[0178] In Table 11, the amount of protein synergist added is 10 mL of the protein adhesion synergist product of Example 10 per 10 L of water, that is, the final concentration of the protein adhesion synergist of Example 27 in the spray is 10 mL / 10 L.

[0179] The experimental results show that the combination of chemical insecticides and the protein synergist of Example 27 has a significant synergistic effect on the control of apple aphids. The control efficacy of the mixture of flonicamid·bifenthrin and the protein synergist was significantly better than the conventional control group at 1, 3, and 7 days, with significant differences in efficacy at 1 and 3 days. The control efficacy of flonicamid·bifenthrin at a 30% reduction and the protein synergist at 1, 3, and 7 days was significantly better than the conventional control group without reduction, and better than the conventional synergist adjuvant Anrongle at 7 days.

[0180] The protein synergist products of Examples 28-30 have been verified to reduce pesticide usage by at least 30%.

[0181] Therefore, the protein synergist product of this application can be reasonably added and used in combination with the insecticide flonicamid·bifenthrin, which can help control apple aphids.

[0182] Test Example 11. Trial of Reduced-Dosage and Enhanced Control of Wheat Fusarium Head Blight by Protein Adhesion Enhancer Products

[0183] The experiment used the protein adhesion enhancer product from Example 11 in a wheat field of Kangmeiyuan Ecological Agriculture Cooperative, Shangguodian Village, Fengxiang District, Baoji City, Shaanxi Province, to conduct a pesticide reduction and efficiency enhancement control trial against wheat scab. The experiment included 9 treatments (Table 12), with each treatment using 30L of water and two applications. The initial disease condition was investigated before application. Because no [further details were provided] at the time of application... The control area was 0.1 mu (approximately 0.067 hectares), with three replicates. The treatment areas were randomly arranged, and the field trial areas were arranged as follows:

[0184] Five samples were taken from each plot, with 100 spikelets surveyed at each point and three replicates. The proportion of diseased spikelets showing spikelet rot symptoms (or white spikelet symptoms caused by stem rot) to all spikelets was classified into five levels.

[0185] Grade 0: Disease-free entire ear;

[0186] Grade 1: Diseased spikelets account for less than 1 / 4 of all spikelets;

[0187] Grade 2: Diseased spikelets account for 1 / 4 to 1 / 2 of all spikelets;

[0188] Grade 3: Diseased spikelets account for 1 / 2 to 3 / 4 of all spikelets;

[0189] Grade 4: Diseased spikelets account for more than 3 / 4 of all spikelets.

[0190] Based on a pre-drug-free disease baseline survey, the preventive efficacy was determined using the following formula:

[0191] Table 12 Experimental Treatments

[0192] Note: Anrongle is a lecithin and vitamin E suspension emulsion, which is commercially available.

[0193] In Table 11, the synergist is diluted 1000 times, which means that the final concentration of the protein adhesion synergist in Example 11 in the spray is 10 mL / 10 L.

[0194] The experimental results showed that no chlorosis, deformity, or seedling death was observed in the wheat in the treatment area 1, 3, 5, and 7 days after pesticide application. No abnormal deaths were observed in the released beneficial insects, ladybugs and hoverflies, and their growth and feeding were normal. This indicates that the 1000-fold dilution of the protein enhancer, mixed with 45% tebuconazole·prochloraz emulsifiable concentrate and 50% thiophanate-methyl suspension, is safe for wheat and has no phytotoxicity, nor does it affect other organisms in the field.

[0195] Seven days after the second application, the overall incidence of wheat scab was mild, with a low rate of diseased ears. The incidence rate in the blank control was 17.29%, while it was 10-11% in the four treatment groups of tebuconazole·prochloraz and 8-9% in the four treatment groups of thiophanate-methyl. Comparing the efficacy data of the commercially available synergist Anrongle (see Figure 11), the control efficacy of the tebuconazole·prochloraz (normal dosage) + Anrongle treatment group was comparable to that of tebuconazole·prochloraz (normal dosage) alone against wheat scab. The control efficacy of tebuconazole·prochloraz (normal dosage) + protein synergist and 30% reduced dosage tebuconazole·prochloraz + protein synergist against wheat scab was significantly better than that of tebuconazole·prochloraz alone. This indicates that the synergistic effect of the protein synergist product of this application when mixed with pesticides is superior to that of the commercially available synergist Anrongle. The control efficacy of thiophanate-methyl at standard dosage + protein synergist and thiophanate-methyl at 30% reduced dosage + protein synergist against wheat scab was superior to that of thiophanate-methyl alone at standard dosage. These results indicate that the rational addition and use of the protein synergist product described in this application can significantly improve the control effect against wheat scab.

[0196] This application allows for the substitution of other pesticides, fertilizers, or biostimulants for the imidacloprid, dinotefuran, pyridaben, thiamethoxam, spinosad, chlorantraniliprole, indoxacarb, oxadixyl-metalaxyl, amino acid-containing foliar fertilizers, etc., in this application. Other plant-derived proteins can also be substituted for the proteins used in Examples 1-30 above, all of which are within the scope of protection of this application.

[0197] Comparative Example 1

[0198] Using animal protein as a film-forming agent: a comparison of the synergistic effects of animal protein (bovine serum albumin, 10 mg / ml) + reducing agent (TCEP, 50 mM) is shown in Figure 12. The results indicate that the synergistic effect of animal protein + reducing agent on the pesticide imidacloprid is lower than that of single plant protein (the protein adhesion synergist in Example 2).

[0199] Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of this application, and are not intended to limit them. Although this application has been described in detail with reference to the foregoing embodiments, those skilled in the art should understand that modifications can still be made to the technical solutions described in the foregoing embodiments, or equivalent substitutions can be made to some of the technical features. Such modifications or substitutions do not cause the essence of the corresponding technical solutions to deviate from the spirit and scope of the technical solutions of the embodiments of this application. Industrial applicability

[0200] This application provides a plant-derived protein-based agrochemical protein adhesion enhancer, its preparation method, and its application. The product comprises the following raw materials in parts by weight: 20-500 parts plant-derived protein, 50-450 parts protein dispersant, and 20-350 parts protein stabilizer. This product improves the utilization rate of agrochemicals, reduces crop yield reduction and environmental pollution caused by agrochemical runoff, and, as the protein degrades into amino acids, promotes plant growth and enhances plant resistance to abiotic stress, achieving reduced usage and increased efficiency of agrochemicals.

Claims

1. A plant-derived protein-based agrochemical protein adhesion synergist, characterized in that, The ingredients contain the following proportions by weight: 20-500 parts plant-derived protein, 50-450 parts protein dispersant, and 20-350 parts protein stabilizer.

2. The agricultural chemical protein adhesion enhancer according to claim 1, characterized in that, The ingredients contain the following proportions by weight: 20-500 parts of plant-derived protein, 50-450 parts of protein dispersant, and 20-350 parts of protein stabilizer. Optionally, the raw materials include the following parts by weight: 200-500 parts of plant-derived protein, 50-200 parts of protein dispersant, and 25-100 parts of protein stabilizer. Optionally, the raw materials include the following parts by weight: 200-500 parts of plant-derived protein, 50-120 parts of protein dispersant, and 25-80 parts of protein stabilizer. Optionally, the raw materials include the following parts by weight: 300-500 parts of plant-derived protein, 50-120 parts of protein dispersant, and 25-50 parts of protein stabilizer. Optionally, the plant-derived protein can spontaneously aggregate at the interface to form a film.

3. The agrochemical protein adhesion enhancer according to claim 1 or 2, characterized in that, The protein dispersant is selected from one or more of the following: polyether sulfonates, chain carboxylate polymers, carboxylate polymers, alkoxy fatty alcohol phosphates, polycarboxylates, sodium lignosulfonate, phosphate esters, alkyl naphthalene sulfonate formaldehyde condensates, naphthalene sulfonates, formaldehyde condensates, long-chain fatty alcohol polyoxyethylene ethers, alkylphenol polyoxyethylene ethers, fatty acid polyoxyethylene esters, polyoxyethylene alkylamines, glycerol fatty acid esters, sorbitol fatty acid esters, dehydrated sorbitol fatty acid esters, sucrose fatty acid esters, sodium alginate, carboxymethyl cellulose, carboxyethyl cellulose, acrylic polymers, polyvinylpyrrolidone, polyacrylamide, anionic surfactants, and nonionic surfactants. And / or, the protein stabilizer is selected from one or more of ethylene glycol, isopropanol, diethyl ether, propylene oxide, toluene, xylene, methyl acetate, ethyl acetate, propyl acetate, pentane, hexane, octane, cyclohexane, cyclohexanone, methylcyclohexanone, chlorobenzene, dichlorobenzene, dichloromethane, acetone, methyl butyl ketone, methyl isobutyl ketone, etc., ethylene glycol monomethyl ether, ethylene glycol monoethyl ether, ethylene glycol monobutyl ether, acetonitrile, pyridine, phenol, pectin, xanthan gum, and other plant / microbial polysaccharides.

4. The agrochemical protein adhesion enhancer according to any one of claims 1 to 3, characterized in that, The plant-derived proteins are selected from any one or more proteins found in the plants listed in the table below:

5. The agrochemical protein adhesion synergist according to any one of claims 1 to 4, characterized in that, The plant-derived proteins mentioned are selected from one or more of the following plant proteins: legumes, grasses, jujubes, roses, madders, convolvulaceae, lindens, solanaceae, asteraceae, cruciferous plants, bryophytes, cucurbits, moraceae, purslane, theaceae, sesamoides, gentians, soapberry, sapotaceae, pinaceae, nymphaeaceae, anabolica, sedges, urticaria, ginger, ginkgo, cypress, burmannii, peony, ephedra, violaceae, dioscoreaceae, brassicaceae, and osderaceae. Optionally, legume proteins include one or more of the following: soybean protein, peanut protein, mung bean protein, kidney bean protein, black bean protein, pea protein, red bean protein, broad bean protein, and alfalfa protein; optionally, grass protein includes one or more of the following: corn protein, oat protein, barley protein, wheat protein, rye protein, buckwheat protein, rice protein, and millet protein; optionally, Osmunda species protein includes bracken protein; optionally, Rosaceae species protein includes one or more of the following: almond protein and papaya protein; optionally, Malvaceae species protein includes one or more of the following: cottonseed protein and okra protein. Optionally, the protein from Convolvulaceae plants includes one or more of purple sweet potato protein and sweet potato protein; Optionally, the protein from Dioscoreaceae plants includes sweet potato protein; Optionally, the protein from Cruciferae plants includes one or more of broccoli protein and rapeseed protein; Optionally, the protein from Cucurbitaceae plants includes one or more of pumpkin protein, cucumber seed protein, pumpkin seed protein, bitter melon protein, and gourd protein; Optionally, the protein from Sapindaceae plants includes one or more of lychee protein and longan / dried longan protein; Optionally, the protein from Nymphaeaceae plants includes lotus seed protein; Optionally, the protein from Bryophyllaceae plants includes water shield protein; Optionally, The proteins from plants in the Urticaceae family include one or more of nettle protein and mulberry leaf protein; optionally, the proteins from the Juglandaceae family include walnut protein; optionally, the proteins from the Linaceae family include flaxseed protein; optionally, the proteins from the Solanaceae family include potato protein; optionally, the proteins from the Asteraceae family include sunflower seed protein; optionally, the proteins from the Bryaceae family include bryophyte protein; optionally, the proteins from the Moraceae family include hemp seed protein; optionally, the proteins from the Portulacaceae family include purslane protein; optionally, the proteins from the Theaceae family include tea protein; optionally, the proteins from the Pseudoaceae family include sesame protein; optionally, the proteins from the Gentianaceae family include gentian protein. White; Optionally, the plant protein from the Sapotaceae family includes avocado protein; Optionally, the plant protein from the Pinaceae family includes pine nut protein; Optionally, the plant protein from the Anacardiaceae family includes cashew nut protein; Optionally, the plant protein from the Cyperaceae family includes sedge protein; Optionally, the plant protein from the Zingiberaceae family includes ginger protein; Optionally, the plant protein from the Ephedra family includes ephedra protein; Optionally, the plant protein from the Ginkgoaceae family includes ginkgo protein; Optionally, the plant protein from the Cupressaceae family includes cypress fruit protein; Optionally, the plant protein from the Burseraceae family includes olive protein; Optionally, the plant protein from the Violaceae family includes violet protein; Optionally, the plant protein from the Paeoniaceae family includes peony protein and rose protein; Optionally, it also includes water, in a content of 200 to 800 parts by weight, or optionally 600 to 800 parts by weight.

6. The agrochemical protein adhesion enhancer according to any one of claims 1 to 5, characterized in that, One or more of the plant-derived proteins are subjected to physical and chemical modification; Optionally, physical modification includes one or more of the following: pH adjustment, salt concentration, heat treatment, ultrasonic treatment, microwave treatment, high pressure treatment, radio frequency treatment, and mechanical stirring. Optionally, chemical modification includes initiating monomer polymerization containing functional groups from the protein, or grafting functional polymers or small molecules onto the protein surface; optionally, the initiating functional groups include one or more of carboxyl, hydroxyl, carbonyl, and amino groups; optionally, the functional polymers used to initiate functional polymerization or grafting include one or more of polyethylene glycol, polyacrylic acid, polylactic acid, and polysaccharides; optionally, the small molecules used to initiate functional polymerization or grafting include polyphenols, polycarboxylic acids, ketones, glycosides, etc. One or more of the following: plant essential oils, nicotine-like substances, and other plant secondary metabolites; optional polysaccharides including one or more of the following: starch, cellulose, algal polysaccharides, chitin / chitosan, plant polysaccharides, microbial polysaccharides, anionic polysaccharides, cationic polysaccharides, and neutral polysaccharides; optional polyphenols including flavonoids such as epicatechin, cyanidin, quercetin, and naringenin; phenolic acids such as gallic acid, caffeic acid, chlorogenic acid, and rhein; stilbene compounds such as resveratrol; stilbene compounds such as jasmonic acid; stilbene compounds such as echinacea extract; and lignans. One or more of the following: tannic acid, etc.; optionally, polycarboxylic acids including one or more of oxalic acid, citric acid, malic acid, glycyrrhizic acid, etc.; optionally, plant essential oils including one or more of tea tree oil, thyme oil, rose oil; chemical modification also includes the introduction of reducing thiol compounds or protein denaturing agents; optionally, reducing thiol compounds including one or more of mercaptoethanol, cysteine, glutathione, mercaptosuccinic acid, dihydrolipoic acid, tris(2-carboxyethyl)phosphohydrochloride; protein denaturing agents including urea, salts The chemical modification includes one or more of guanidine acid, guanidine isothiocyanate, sodium dodecyl sulfate, and arginine; the chemical modification also includes enzymatic cross-linking or degradation, wherein the cross-linking enzymes include one or more of transglutaminase, oxidases (tyrosinase, laccase, peroxidase, thiol oxidase), lipoxygenase, and gamma-glutamyl endopeptidase; the oxidases include one or more of tyrosinase, laccase, peroxidase, and thiol oxidase; and the degrading enzymes include one or more of papain, bromelain, and soybean protease.

7. An agricultural chemical formulation, characterized in that, It includes agricultural chemicals and the agricultural chemical protein adhesion enhancers as described in any one of claims 1 to 6; optionally, agricultural chemicals include one or more of pesticides, fertilizers, and biostimulants.

8. The agrochemical formulation according to claim 7, characterized in that, Pesticides include one or more of the following: insecticides, fungicides, antiviral agents, herbicides, acaricides, nematicides, rodenticides, plant growth regulators, insect growth regulators, plant immune inducers, fumigants, biological pesticides, mineral-derived pesticides, organic synthetic pesticides, and seed dressing agents. And / or, fertilizers include one or more of the following: organic fertilizers, chemical fertilizers, compound fertilizers, slow-release fertilizers, bio-fertilizers, micronutrient fertilizers, foliar fertilizers, soil conditioners, and organic-inorganic compound fertilizers. And / or, biostimulants include one or more of the following: humic acid substances, seaweed extracts, free amino acids, complex organic matter, non-organic minerals, microorganisms and their secondary metabolites, plant extracts and their secondary metabolites, chitin and chitosan derivatives, beneficial chemical elements, and antitranspirants. Optionally, the target surface of the agrochemical is any one of the following: the surface of an insect body, plant leaves, plant roots and stems, or seed surface; Optionally, the concentration of the agricultural chemical protein adhesion enhancer is 5–20 mL / 10 L, or optionally 10 mL / 10 L.

9. A method for preparing an agricultural chemical protein adhesion synergist according to any one of claims 1 to 6, or an agricultural chemical formulation according to any one of claims 7, comprising the following steps: 1) First, add the plant-derived protein to 200-800 parts of deionized water, then add the protein dispersant and disperse and mix. 2) Add the protein stabilizer to the protein mixture obtained in step 1), and homogenize it by shearing and sand milling to obtain a stable plant-derived protein adhesive; optionally, stable plant-derived protein adhesives of different grades from 3nm to 60nm can be obtained.

10. The application of a plant-derived protein in the preparation of agrochemical protein adhesion synergists, characterized in that, The plant-derived proteins mentioned are selected from one or more of the following plant proteins: legumes, grasses, jujubes, roses, madders, convolvulaceae, linnaceae, solanaceae, asteraceae, cruciferous plants, bryophytes, cucurbits, moraceae, purslane, theaceae, sesamoides, gentians, soapberry, sapotaceae, pinaceae, nymphaeaceae, anabolica, sedges, urticaria, ginger, ginkgo, cypress, olive, peony, ephedra, violaceae, dioscoreaceae, brassicaceae, and ospermaceae.

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