Modification of wheat gluten for improvement of binding capacity with keratin in hair

Authors

Shukun Wang, Jiangnan University
Danyang Meng, Jiangnan University
Sisi Wang, Jiangnan University
Zhong Zhang, University of Nebraska–Lincoln
Ruijin Yang, Jiangnan University
Wei Zhao, Jiangnan UniversityFollow

ORCID IDs

Shukun Wang, 0000-0002-6580-5833

Document Type

Article

Date of this Version

1-2018

Citation

Wang S, Meng D,Wang S, Zhang Z, Yang R, ZhaoW. 2018 Modification of wheat gluten for improvement of binding capacity with keratin in hair. R. Soc. open sci. 5: 171216.

doi 10.1098/rsos.171216

Comments

Copyright (c) 2018 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License

Abstract

In this study, enzymatic hydrolysis and cationization with epoxypropyldodecyldimethylammonium chloride of wheat protein, an economic protein complex containing great amount of disulfide bonds, were conducted to improve properties such as solubility and disassociation behaviour for recovery of damaged hair when used in shampoo. The optimal conditions for enzymatic hydrolysis were pH 8.2, 55°C with Alcalase for 60min. After the selected hydrolysis, the degree of hydrolysis, nitrogen solubility index, foaming capacity index, foam stability index, emulsifying activity index and emulsion stability index of hydrolysate with 58.71% of shortchain peptides (less than 1000 Da) were 8.81%, 39.07%, 225%, 56.67%, 9.62m² g⁻¹ and 49.08, respectively. The cationization was followed to raise the isoelectric point of wheat protein hydrolysate from 7.0 to 10.0, which could facilitate the quaternized protein hydrolysate to adhere to the surface of hair at the range of pH 5–6 of hair care products to form more disulfide bonds. The results show that a shampoo with quaternized wheat proteins hydrolysate possesses excellent properties in recovering damaged hair, making the surface of hair smooth and compact.