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Surface activity of pepsin‐solubilized collagen acylated by lauroyl chloride along with succinic anhydride
Author(s) -
Li Conghu,
Liu Wentao,
Duan Lian,
Tian Zhenhua,
Li Guoying
Publication year - 2014
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.40174
Subject(s) - succinic anhydride , emulsion , chemistry , acylation , surface tension , absorption of water , absorption (acoustics) , acetic anhydride , wetting , chromatography , nuclear chemistry , polymer chemistry , organic chemistry , materials science , catalysis , physics , quantum mechanics , composite material
The surface activity of pepsin‐solubilized type I collagen acylated by lauroyl chloride and succinic anhydride was investigated in this article. Compared with native collagen, acylated collagen exhibited better surface activity such as oil absorption capacity, emulsion activity and stability, foam expansion, and foam stability but presented lower water absorption capacity. Acylated collagen also had higher emulsion activity and stability than Tween 80, whereas Tween 80 displayed higher foam expansion and stability than acylated collagen. After acylation, the surface tension of collagen decreased with the storage time increased, the hydrophobicity and the wetting power increased with the increase of the concentration. Meanwhile, the emulsion activity and stability of acylated collagen decreased with the increase of NaCl concentration ranging from 20 to 100 mmol/L. Under neutral pH value, acylated collagen reached higher emulsion activity and stability at acylated collagen concentration of 0.4 mg/mL and lower temperature (<35°C). © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014 , 131 , 40174.

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