10 results about "Cutinase" patented technology

The invention relates to the technical field of enzyme engineering and recombinant protein expression, and discloses a mutant for improving cutinase yield and a preparation method thereof. The mutant protein is based on an amino acid sequence as shown in SEQ ID NO.1 and has G93Q or H209F single-point substitution, and the site number takes first methionine in the SEQ ID NO.1 as the first site. The invention also provides a nucleic acid molecule for coding the mutant, a recombinant expression vector and a recombinant host cell, and a method for adding an inducer to induce expression when OD600 is 0.6-1.2 in a culture process so as to obtain a culture containing the mutant. Embodiments show that the enzyme activity per unit volume of the mutant culture is higher than that of a control group.

The present invention relates to a method for treating a textile comprising a polyester with low crystallinity by contacting the textile with a cutinase, as well as a textile produced by such method.

This invention discloses a BhrPETase keratinase mutant and its application in the degradation of polyethylene terephthalate (PET), belonging to the fields of environmental science and enzyme engineering. The site numbers are based on the amino acid sequence shown in SEQ ID NO:1. The mutant contains substitutions of S14G, H78Y, and S184G relative to SEQ ID NO:1, with the preferred amino acid sequence shown in SEQ ID NO:9. Under conditions of 1 mg enzyme protein / g substrate, 65°C, and 96 h, the preferred mutant exhibits a degradation rate of 90.4% for PET membranes and a half-life of 150 h at 60°C, making it suitable for enzymatic degradation and depolymerization of PET.

The invention discloses a cutinase mutant and application thereof in degradation of polyethylene glycol terephthalate, and belongs to the field of environmental science. According to the present invention, BhrPETase derived from bacteria HR29 and LC cutinase of a metagenome in plant compost are modified to obtain mutants, the mutants are subjected to single-point or multi-point mutation near the substrate binding site of the BhrPETase or the LC cutinase, and the 184th site and the 156th site are subjected to single-point mutation or combined mutation to construct six mutants; compared with a wild type enzyme, the six mutants (M1-M6) have the advantages that the enzyme activity and the PET degradation efficiency are obviously improved, and the industrial prospect is good.

The application discloses a wool tricarboxylic acid blended fabric and a preparation method thereof, and belongs to the technical field of textile printing and dyeing. The method comprises the following steps: respectively performing normal-pressure low-temperature plasma pretreatment and specific enzyme synergistic modification on wool sliver and tricarboxylic acid short fiber sliver, moderately passivating wool scales by using protease, and promoting surface micro-deacetylation of tricarboxylic acid by using esterase or cutinase; mixing the slivers, spinning and weaving into a fabric; performing one-bath same-color dyeing by using disperse / acid dyes at 100 DEG C under normal pressure; and performing medium-low temperature heat setting. Through synergistic effect of plasma physical etching and biological enzyme chemical degradation, the technical prejudice that tricarboxylic acid needs high-temperature dyeing at 130 DEG C is broken. The method can obtain excellent same color under normal pressure, significantly improves wool strength retention rate, avoids wool heat damage and yellowing, the finished product has low shrinkage rate after machine washing, is green and environment-friendly, and is suitable for industrial popularization.

The application discloses a method for improving catalytic degradation of PET plastic by cutinase, and the method comprises the following steps: preparing a high-molecular condensed phase, collecting a concentrated phase of the condensed phase by centrifugation, adding LCC-ICCG-218Y enzyme solution and PET solid to the concentrated phase, and oscillating to make the concentrated phase uniformly distributed in the reaction system, starting the reaction under oil bath at 40-72 DEG C, collecting the reaction liquid, and characterizing the degradation product of the reaction liquid by ultraviolet. Compared with a phosphate buffer solution, the degradation rate of PET plastic at 40 DEG C and 50 DEG C is finally doubled. The method establishes a simple method for improving enzymatic hydrolysis of PET plastic, and only by adjusting the reaction microenvironment of the enzyme, without complex protein modification and enzyme immobilization means, the method has certain application value.

The invention discloses a cutinase mutant with remarkably enhanced catalytic efficiency on polyvinyl acetate and application of the cutinase mutant, and belongs to the technical field of enzyme engineering and genetic engineering. The combined mutant C11 provided by the invention shows that the catalytic efficiency on polyvinyl acetate is obviously improved, and the yield of a degradation product acetic acid is 1.73 times that of M8. In addition, the half-life period of C11 at 70 DEG C is 205.9 hours, and the half-life period is prolonged by 5.17 times compared with the half-life period of M8. Meanwhile, the stability of the C11 in an alkaline environment is enhanced, so that the C11 has higher alkali resistance, and the application potential of the C11 under an alkaline condition is widened. The cutinase mutant provided by the invention represents a biocatalyst which has a great prospect in application of industrial paper pulp and paper.

The invention relates to the technical field of diglyceride preparation, in particular to a preparation method of diglyceride with a uric acid reducing effect. Comprising the following steps: (1) vegetable oil is partially hydrolyzed with a complex enzyme composed of lipase and cutinase, a hydrolysate is obtained after dehydration, and the content of free fatty acid in the hydrolysate is 37.0 wt%-46.0 wt%; and (2) adding glycerol and lipase into the hydrolysate obtained in the step (1) to react, adding water to remove excessive glycerol, standing for layering, collecting supernatant, and carrying out distillation separation to obtain the edible diglyceride. The content of diglyceride in the final product reaches 80% or above by strictly controlling enzyme composition and free fatty acid in the hydrolysis and esterification processes, the reaction process is carried out according to the hydrolysis and esterification sequence, the process steps are simple, no organic solvent is used in the whole reaction process, green and environment-friendly effects are achieved, and the obtained diglyceride has a remarkable uric acid reducing effect.

The invention belongs to the technical field of treatment of textiles or analogues, and particularly relates to the technical field of washing of fiber products, in particular to a preparation method of a machine washable cashmere sweater. The method comprises the following steps: cleaning cashmere fibers containing skin to obtain cleaned fibers; the bath ratio for cleaning is 1: (20-50); the use amount of a detergent used for cleaning is 1-2.5% (o.w.f); the cleaning comprises ultrasonic cleaning, and the frequency of the ultrasonic cleaning is 17-50 kHz; the power of ultrasonic washing is 0.3-0.5 W / cm < 3 >; the cleaning time is 2 to 15 minutes; performing enzyme treatment on the cleaned fibers by using a compound enzyme solution to obtain enzyme treated fibers; the compound enzyme solution comprises cutinase, and the using amount of the cutinase is 4-10 mL / g; the enzyme treatment time is 5-6 hours; adjusting the pH value of the compound enzyme solution to 8-8.5 by using a buffer solution; the fiber bath ratio after cleaning is 1: (20-50). According to the method, heavy non-protein components of the skin are directionally decomposed through specific low-frequency ultrasonic waves in cooperation with single-component cutinase, the skin removal rate is increased, and then the machine washable capacity of the cashmere sweater is improved through a series of treatment methods.

The invention discloses a cutinase mutant gene, a protein expressed by the cutinase mutant gene and application of the cutinase mutant gene. The protein expressed by the cutinase mutant gene can be correctly folded and can be massively purified in an escherichia coli system. Meanwhile, the mutant protein disclosed by the invention has the function of degrading PET (Polyethylene Terephthalate) by wild cutinase, and the catalytic efficiency of the protein expressed by the cutinase mutant gene is improved compared with that of a control group. The protein expressed by the keratin mutant gene has activity and stability at 40-80 DEG C. Specifically, when the pH value is 8.0 and the temperature is 72 DEG C, the PET degradation capacity is improved by 20% compared with that of a control group, and when the pH value is 8.0 and the temperature is 60 DEG C, the PET degradation capacity is improved by 70% compared with that of the control group.