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Isolation and characterization of collagen from bigeye snapper ( Priacanthus macracanthus ) skin
Author(s) -
Jongjareonrak Akkasit,
Benjakul Soottawat,
Visessanguan Wonnop,
Tanaka Munehiko
Publication year - 2005
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2072
Subject(s) - acetic acid , protease , pepsin , chemistry , solubility , peptide , biochemistry , proline , chromatography , enzyme , amino acid , organic chemistry
Acid‐solubilized collagen (ASC) and pepsin‐solubilized collagen (PSC) were isolated from the skin of bigeye snapper ( Priacanthus macracanthus ) with yields of 64 and 11 g kg −1 wet weight, respectively. Both ASC and PSC were characterized as type I collagens with no disulfide bonds. Peptide maps of ASC and PSC digested by V8 protease and lysyl endopeptidase showed some differences in peptide patterns and were totally different from those of calf skin collagen. The maximum solubility was observed at pH 4 and 5 for ASC and PSC, respectively. A sharp decrease in solubility of both collagens in acetic acid was found with NaCl concentration above 30 g l −1 . Thermal transitions of ASC and PSC in deionized water were observed with T max of 30.37 and 30.87 °C, respectively, and were lowered in the presence of acetic acid (0.05 mol kg −1 solution). Therefore, ASC was a major fraction in bigeye snapper skin and it exhibited some different characteristics to PSC. Copyright © 2005 Society of Chemical Industry