Antibacterial Functionalization of Wool via mTGase-Catalyzed Grafting of ε-Poly-L-lysine

被引:27
作者
Wang, Qiang [1 ]
Jin, Guibiao [1 ]
Fan, Xuerong [1 ]
Zhao, Xianfei [1 ]
Cui, Li [1 ]
Wang, Ping [1 ]
机构
[1] Jiangnan Univ, Minist Educ, Key Lab Sci & Technol Ecotext, Wuxi 214122, Jiangsu, Peoples R China
基金
国家高技术研究发展计划(863计划);
关键词
Microbial transglutaminase (mTGase); Antibacterial functionalization; Enzyme-catalyzed grafting; epsilon-Poly-L-lysine; Wool; TENSILE-STRENGTH; TRANSGLUTAMINASE; TEXTILES; ENZYME; POLYLYSINE;
D O I
10.1007/s12010-009-8708-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
epsilon-Poly-L-lysine (epsilon-PL), a natural biomacromolecule having a broad spectrum of antibacterial activity, was grafted on the wool fiber via the acyl transfer reaction catalyzed by microbial transglutaminase (mTGase) to develop a new strategy for antibacterial functionalization of proteinous materials. The effects of the concentrations of epsilon-PLs and mTGases on the graft yields were investigated. A coating of epsilon-PL that almost completely covered the scale profile on the wool surface was visualized by scanning electron microscopy (SEM) and further demonstrated in terms of Allworden's reaction characteristic of wool. Identifiable differences in lysine content and color depth among the stained wool samples reveal the changes in the surface composition and polarity caused by the incorporation of epsilon-PL onto the wool substrate, respectively. The ratio of bacteriostasis to Escherichia coli of the wool fabric grafting epsilon-PL reached 96.6%, indicating an excellent antibacterial effect. The application of epsilon-PL and corresponding mTGase-catalyzed grafting reaction would provide a worthwhile reference for antibacterial functionalization of proteinous materials in various forms.
引用
收藏
页码:2486 / 2497
页数:12
相关论文
共 29 条
[1]  
Arrizubieta M.J., 2007, IND ENZYMES STRUCTUR, P567
[2]   Enzyme-mediated crosslinking of wool. Part II: Keratin and transglutaminase [J].
Cardamnone, Jeanette M. ;
Phillips, John G. .
TEXTILE RESEARCH JOURNAL, 2007, 77 (05) :277-283
[3]  
Cavaco-Paulo ArturGubitz G. M., 2003, TEXTILE PROCESSING E
[4]   Application of transglutaminases in the modification of wool textiles [J].
Cortez, J ;
Bonner, PLR ;
Griffin, M .
ENZYME AND MICROBIAL TECHNOLOGY, 2004, 34 (01) :64-72
[5]   Transglutaminase mediated grafting of silk proteins onto wool fabrics leading to improved physical and mechanical properties [J].
Cortez, Joao ;
Anghieri, Anna ;
Bonner, Philip L. R. ;
Griffin, Martin ;
Freddi, Giuliano .
ENZYME AND MICROBIAL TECHNOLOGY, 2007, 40 (07) :1698-1704
[6]   Improvement of shrink-resistance and tensile strength of wool fabric treated with a novel microbial transglutaminase from Streptomyces hygroscopicus [J].
Du, Guocheng ;
Cui, Li ;
Zhu, Yang ;
Chen, Jian .
ENZYME AND MICROBIAL TECHNOLOGY, 2007, 40 (07) :1753-1757
[7]  
Freddi G, 2001, J APPL POLYM SCI, V82, P3513, DOI 10.1002/app.2213.abs
[8]   Recent advances in antimicrobial treatments of textiles [J].
Gao, Yuan ;
Cranston, Robin .
TEXTILE RESEARCH JOURNAL, 2008, 78 (01) :60-72
[9]   Transglutaminases: Nature's biological glues [J].
Griffin, M ;
Casadio, R ;
Bergamini, CM .
BIOCHEMICAL JOURNAL, 2002, 368 :377-396
[10]   Antimicrobial activity of wool fabric treated with curcumin [J].
Han, SY ;
Yang, Y .
DYES AND PIGMENTS, 2005, 64 (02) :157-161