Dissertation
Dissertation > Industrial Technology > Light industry,handicrafts > Textile industry,dyeing and finishing industry > Dyeing and finishing industry > Finishing > Chemical finishing

The Study of the Mechanism Transglutaminase’s Bio-Modification on Wool

Author GongJiaJia
Tutor WangShuGen
School Jiangnan University
Course Textile Engineering
Keywords microbial transglutaminase wool casein indophenol blue spectrophotometric method electrop
CLC TS195.5
Type Master's thesis
Year 2010
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Transglutanunase (TG) is an enzyme capable of catalyzing acyl transfer reactions by Introducing covalent crossing-links among proteins as well as peptides and various primary amines .The wool fibers mainly consist of protein and amino acid ,like glutamic acid and lysine .With the transglutaminase,the crosslink of proteins in wool fibers can be formed. Chlorine or its derivatives is often used in traditional modification of wool. AOX (absorbable organic halogen) in chlorinating processes causes seriously environmental pollution. Then some methods are developed in wool modification.In this paper, indophenol blue method is used to determinate the product (ammonium) of MTG-catalyzed reactions of wool fabrics. The impact of different buffer systems for the indophenol blue method was first studied. It was found that Tris-HCl buffer solution is unsuitable for this method, while phosphate buffer solution has less effect. Compared the whiteness and breaking strength of the MTG-catalyzed wool fabrics with the ammonia content of the reaction residue, we found the breaking strength is repaired 6% and 4% respectively. And the whiteness is repaired 2% of the wool fabric dealed with DCCA. But we can’t detect the ammonia in the reaction system. So we known that the indophenol blue method is not sufficient exact because of the little releasetion of the MTG-catalyzed reactions of wool fabrics. Upon that we study the wool’s simulant (caseins) and confirm that MTG can be useful to caseins. It’s detected 7.5μg/ml ammonia when the enzyme concentration is at 10g/L. At last , we confirm that MTG can be useful to the wool keratins we made ourselves. It’s detected 2.5μg/ml ammonia when the enzyme concentration is at 16g/L. It was also found that reducing agent DTT could improve the MTG-catalyzed reaction for wool keratin when the concentration is at 20mmol/L. Based on the SDS-PAGE electrophoresis and infrared spectroscopy, we also proved the MTG-catalyzed reactions of caseins and wool keratins

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