Method for preparing bioactive peptide from canned fish production waste liquid

A technology of biologically active peptides and waste liquids, applied in the preparation methods of peptides, chemical instruments and methods, and medical preparations containing active ingredients, etc. Reduced production cost, high economy, good effect of ACE inhibitory activity

Inactive Publication Date: 2017-03-15
FUZHOU UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] A large amount of cooking liquid will be produced in the production process of canned fish. At present, due to the lack of effective technical means in enterprises, the cooking liquid for the processing of protein-rich canned fish is rarely used, and most of them are directly discharged. This not only causes waste of resources, but also affects Serious pollution of marine and terrestrial environments

Method used

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  • Method for preparing bioactive peptide from canned fish production waste liquid
  • Method for preparing bioactive peptide from canned fish production waste liquid
  • Method for preparing bioactive peptide from canned fish production waste liquid

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0024] Embodiment 1 Determination of compound enzyme reaction system

[0025] The four reaction systems compounded by alkaline protease and trypsin are shown in Table 1. The enzymatic hydrolysis effects of different reaction systems were investigated with the hydroxyl radical scavenging rate as an index. The results are shown in figure 1 .

[0026] Table 1 Different complex enzyme reaction systems

[0027]

[0028] Such as figure 1 As shown, the effect of system 4 is the best, that is, trypsin is firstly added for reaction, the reaction temperature is 55 ℃, and the time is 4 h; then alkaline protease is added for reaction, the reaction temperature is 60 ℃, the time is 3 h, the corresponding The hydroxyl free radical inhibition rate is as high as 61%, which is 21.47% higher than the result of alkaline protease single-enzyme hydrolysis (39.53%), 40.17% higher than the result of trypsin single-enzyme hydrolysis (19.83%), and higher than alkaline protease and The sum of the ...

Embodiment 2

[0029] Embodiment 2 Composite enzyme hydrolyzate molecular weight distribution

[0030] Add trypsin in the amount of 7450 U / g to the waste liquid of canned fish production, react at 55°C and pH 8 for 4 h; Continue to react for 3 hours, use TSK-gelG3000sw chromatographic column to analyze the molecular weight of the enzymatic hydrolysis product, the results are as follows figure 2 , Table 2.

[0031] Table 2 HPLC analysis results of compound enzyme hydrolysis products

[0032]

[0033] It can be seen from Table 2 that after hydrolysis with alkaline protease and trypsin, the components with a molecular weight of less than 1 KDa accounted for 50% of the product, which was higher than that of alkaline protease (30%) and trypsin (28%) The effect of enzymatic hydrolysis shows that the use of segmented compound enzymatic hydrolysis can greatly increase the yield of small molecule peptides.

Embodiment 3

[0034] Example 3 Study on the Activity of Compound Enzyme Hydrolyzate

[0035] Using ultrafiltration membranes with different cut-offs (10 KDa, 3 KDa, 1 KDa) to separate the complex enzyme hydrolysis products, the molecular weight is <1 KDa (P1), 1 KDa-3 KDa (P2), 3 KDa-10 KDa (P3) of the three components.

[0036] 1. Antioxidant activity research

[0037] 1.1 Hydroxyl free radical inhibition experiment

[0038] The curve of the inhibitory effect of the three components in the compound enzyme hydrolyzate on hydroxyl radicals as a function of concentration is shown in image 3 .

[0039] Depend on image 3 It can be seen that all three components have inhibitory effects on hydroxyl radicals, and the increase of the inhibitory rate is positively correlated with the dose of the components; among them, the inhibitory effect of P1 component on hydroxyl free radicals is relatively good.

[0040] 1.2 DPPH free radical inhibition experiment

[0041] The curve of the inhibitory e...

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PUM

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Abstract

The invention discloses a method for preparing bioactive peptide from canned fish production waste liquid, belonging to the field of food biotechnology. The method comprises the following steps of: with the canned fish production waste liquid as a raw material, hydrolyzing with a compound enzyme (alkaline protease and trypsin), and separating with an ultrafiltration membrane to obtain small-molecular-weight bioactive peptide with antioxidant activity and ACE inhibitory activity. The method disclosed by the invention is conductive to realizing high-value utilization of the canned fish production waste liquid, can greatly reduce the production cost of biological peptide products and brings relatively high economic, ecological and social benefits.

Description

technical field [0001] The invention belongs to the field of food biotechnology, and in particular relates to a method for preparing small-molecular-weight biologically active peptides by using waste liquid from canned fish production. Background technique [0002] Antioxidant peptide is a general term for a class of peptides with antioxidant activity or reducing activity, which can remove excess free radicals produced by the body, reduce the content of peroxides in the body and the rate of autoxidation, and effectively prevent the body from damage caused by the accumulation of free radicals. damage. Although natural antioxidant peptides extracted from living organisms, such as glutathione, carnosine, and anserine, can be directly isolated and utilized, the current extraction of natural antioxidant peptides is far from meeting the needs of consumers for antioxidants. [0003] Hypertension is a relatively common cardiovascular disease. In the world, especially in developed r...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12P21/06C07K1/34A23L29/00A23L33/18A61K38/01A61P39/06A61P9/12
CPCA23V2002/00A61K38/012C07K1/34C12P21/06A23V2200/02A23V2200/326A23V2250/55
Inventor 林娟毕丹丹郭耀湘叶秀云
Owner FUZHOU UNIV
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