journal article·2017-01-01Open access

Keratinase H328 and Keratinase H328-Proteinase K Treatments for Wool Surface

Chendi Tu, Fusako Kawai, Kunihiko Watanabe, Kiyomi Okada, Sachiko Sukigara

Abstract

Environmentally friendly modification of the wool cuticle to enhance wool fabric comfort is an important goal for the industry. The present study describes the effect of a keratinase from Meiothermus ruber H328 (Keratinase H328) on wool fiber keratin. Keratinase H328 treatment corroded the wool scale. The effect was characterized by physicochemical analyses using scanning electron microscopy (SEM), amino acid analysis, and Fourier-transform infrared-attenuated total reflectance (FTIR-ATR). Subsequently, Keratinase H328 treatment was combined with Proteinase K treatment for the wool fabric. Enzymatically treated wool fabric showed a higher moisture regain than its control at 80% and 90% R.H. The keratinase-proteinase treatment reduced the maximum tensile strain and maximum stress without altering Youngʼs modulus significantly.
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Research context

OpenAlex topics: Enzyme Production and Characterization · Dyeing and Modifying Textile Fibers · Silk-based biomaterials and applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Advanced Fibro-Science, Kyoto Institute of Technology

Center for Fiber and Textile Science, Kyoto Institute of Technology

Division of Applied Life Sciences, Kyoto Prefectural University

Department of Chemical Engineering, Kyoto University

References (22)

Show source-provided references
1. [1] A. N. Parbhu, W. G. Bryson and R. Lal. Biochemistry, 38, 11755–11761 (1999).10.1021/bi990746d ↗
2. [2] J. M. Cardamone and J.Yao. Text Res J , 74, 565–570 (2004).10.1177/004051750407400701 ↗
3. [3] J. D. Leeder and I. C. Watt. J Soc Dyes Colour, 83,226–230 (2008).10.1111/j.1478-4408.1967.tb02765.x ↗
4. [4] P. Senthilkumar, C. Vigneswaran and P. Kandhavadivu. Fibers Polym., 16, 397–403 (2015).10.1007/s12221-015-0397-y ↗
5. [5] A.Bahi,J.T.Jones,C.M.Carr,etal.Text Res J, 77,937–945 (2007).10.1177/0040517507083520 ↗
6. [6] A. Kantouch, H. El-Sayed and A. El-Sayed. J Text Inst, 98, 65–71 (2007).10.1533/joti.2005.0249 ↗
7. [7] A. J. Faenworth. J Soc Dyes Colour, 77, 489–495 (2008).10.1111/j.1478-4408.1961.tb02404.x ↗
8. [8] C. W. Kan and C. W. M. Yuen. J Mater Process Technol, 178, 52–60 (2006).10.1016/j.jmatprotec.2005.11.018 ↗
9. [9] C. X. Wang, M. Du, J.C. Lv et al. Fibers Polym, 16,404–412 (2015).10.1007/s12221-015-0404-3 ↗
10. [10] A. Kaur and J. N. Chakraborty. J Cleaner Prod, 108, 503–513 (2015).10.1016/j.jclepro.2015.07.147 ↗
11. [11] M. Arami, F. Mazaheri and M. J. Beglou. Fibers Polym, 10, 611–616 (2009).10.1007/s12221-010-0611-x ↗
12. [12] Polym, 10P. Wang, Q. Wang, L. Cui, et al. Fibers Polym, 11, 586–592 (2010).10.1007/s12221-010-0586-9 ↗
13. [13] A. Erlacher, F. Sousa, M. Schroeder, et al. Biotechnol Lett, 28, 703–710 (2006).10.1007/s10529-006-9047-1 ↗
14. [14] E. Smith and J. Shen. J Biotechnol, 156, 134–140 (2011).10.1016/j.jbiotec.2011.08.012 ↗
15. [15] S. B. Cai, Z. H. Huang, X. Q. Zhang, et al. Appl Biochem Biotechnol, 163, 112–126 (2011).10.1007/s12010-010-9021-1 ↗
16. [16] B. Liu, J. Zhang, B. Li, et al. World J Microbiol Biotechnol, 29, 825–832 (2013).10.1007/s11274-012-1237-5 ↗
17. [17] J. Fu, J. Su, P. Wang, et al. Appl Microbiol Biotechnol, 99, 10387–10397 (2015).10.1007/s00253-015-6970-x ↗
18. [18] T. Matsui, Y. Yamada, H. Mitsuya, et al. Appl Microbiol Biotechnol, 82, 941–950 (2009).10.1007/s00253-009-1880-4 ↗
19. [19] M. Okamoto, Y. Yonejima, Y. Tsujimoto et al. Appl Microbiol Biotechnol, 57, 103–108 (2001).
20. [20] J.Kunert.A.allg.Mikrobiol. 16, 97–105 (1976).10.1002/jobm.3630160203 ↗
21. [21] N. Eslahi, F. Dadashian and N.H. Nejad. Adv Powder Technol, 24, 416–426 (2013).10.1016/j.apt.2012.09.004 ↗
22. [22] S. Hutchinson, D. Evans, G. Corino et al. Enzyme Microb Technol, 40, 1794–1800 (2007).10.1016/j.enzmictec.2007.01.016 ↗