A novel “trifunctional protease” with reducibility, hydrolysis, and localization used for wool anti-felting treatment
- 112 Downloads
Proteases can cause unacceptable fiber damage when they are singly applied to wool anti-felting treatment which can make wool textiles machine-washable. Even if protease is attached by synthetic polymers, the modified protease plays a limited role in the degradation of keratin with dense structure consisting of disulfide bonds in the scales. Here, to obtain “machine-washable” wool textiles, a novel “trifunctional protease” with reducibility, hydrolysis, and localization is developed by means of covalent bonding of protease molecules with poly (ethylene glycol) bis (carboxymethyl) ether (HOOC-PEG-COOH) and l-cysteine using carbodiimide/N-hydroxysuccinimide (EDC/NHS) coupling, aiming at selectively degrading the scales on the surface of wool. The formation of polymer is confirmed with size exclusion chromatography (SEC) and Fourier transform infrared spectroscopy (FT-IR). Ellman’s test and fluorescence microscopy reveal that the modified protease can reduce disulfide bonds and restrict hydrolysis of peptide bonds on the wool scales. Furthermore, when applied to wool fabrics, the modified protease reach better treatment effects considering dimensional stability to felting (6.12%), strength loss (11.7%) and scale dislodgement proved by scanning electron microscopy (SEM), alkali solubility, wettability, and dyeability. This multifunctional enzyme is well-designed according to the requirement of the modification of wool surface, showing great potential for eco-friendly functionalization of keratin fibers rich in disulfide linkage.
KeywordsProtease modification PEG wool anti-felting
This study was funded by the National Key R&D Program of China (2017YFB0309200), the National Natural Science Foundation of China (51673087, 31771039), the Program for Changjiang Scholars and Innovative Research Teams in Universities (IRT_15R26), Fundamental Research Funds for the Central Universities (JUSRP51717A), and national first-class discipline program of Light Industry Technology and Engineering (LITE2018-21).
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
This article does not contain any studies with human participants or animals performed by any of the authors.
Informed consent was obtained from all individual participants included in the study.
- Chen R, Yuan J, Yu Y, Fan X, Wang Q, Zhu Y (2012) Preparation of chitosan conjugated protease used for shrink resistance of wool and its properties. J food Sci Biotechnolo 31(5):63–68. https://doi.org/10.13560/j.cnki.biotech.bull.1985.2012.02.030 CrossRefGoogle Scholar
- Kynclova E, Elsner E, Kopf A, Hawa G, Schalkhammer T, Fritz P (1996) Novel method for coupling of poly(ethyleneglycol) to carboxylic acid moieties of proteins. J Mol Recognit 9(5–6):644–651. https://doi.org/10.1002/(SICI)1099-1352(199634/12)9:5/6<644::AID-JMR314>3.0.CO;2-7 CrossRefPubMedGoogle Scholar
- Liu B, Zhang J, Li B, Liao X, Du G, Chen J (2013) Expression and characterization of extreme alkaline, oxidation-resistant keratinase from Bacillus licheniformis in recombinant Bacillus subtilis WB600 expression system and its application in wool fiber processing. World J Microb Biot 29(5):825–832. https://doi.org/10.1007/s11274-012-1237-5 CrossRefGoogle Scholar
- Zhu Y, Fan X, Wang Q, Chen R, Yu Y, Yuan J (2011) Chemical modification of Savinase by dextran and its properties. China Biotechnol 31(10):45–49 doi: https://doi.org/10.13523/j.cb.20111009