TY - JOUR
T1 - Alcalase assisted production of novel high alpha-chain gelatin and the functional stability of its hydrogel as influenced by thermal treatment
AU - Zhang, Yi
AU - Dutilleul, Pierre
AU - Orsat, Valerie
AU - Simpson, Benjamin K.
N1 - Publisher Copyright:
© 2018
PY - 2018/10/15
Y1 - 2018/10/15
N2 - High alpha-chain (α-chain) content is associated with superior quality gelatin. In this study, a production process involving mild alcalase treatment was optimized by response surface methodology, and the α-chain was quantified based on SDS-PAGE. A novel fish skin gelatin high in α-chain (32% of total protein, 45 mg/g fish skin of yield) was produced at optimum conditions, i.e., 2.3 U/g alcalase addition to fish skin for 0.5 h at 25 °C, followed by water extraction at 67 °C for 7 h. The novel gelatin contained 34% glycine and 16% imino acids as determined by UPLC. FTIR analysis disclosed four characteristic infra-red amide absorption bands. DSC and TGA analysis revealed thermal decomposition at 215 °C. Novel gelatin hydrogel (1%, w/v) could withstand a wide range of temperatures, and exhibited high emulsifying activity and viscosity, as well as stable gel clarity from 35 °C to 80 °C. The high temperature treatment (95 °C) produced hydrogel with lower clarity and emulsifying activity but higher viscosity than at the other temperatures. All heat-treated gelatin hydrogels behaved as non-Newtonian fluids as per the Ostwald de Waele model. The novel high α-chain fish skin gelatin has potential broad application in food, pharmaceutical and biological industries.
AB - High alpha-chain (α-chain) content is associated with superior quality gelatin. In this study, a production process involving mild alcalase treatment was optimized by response surface methodology, and the α-chain was quantified based on SDS-PAGE. A novel fish skin gelatin high in α-chain (32% of total protein, 45 mg/g fish skin of yield) was produced at optimum conditions, i.e., 2.3 U/g alcalase addition to fish skin for 0.5 h at 25 °C, followed by water extraction at 67 °C for 7 h. The novel gelatin contained 34% glycine and 16% imino acids as determined by UPLC. FTIR analysis disclosed four characteristic infra-red amide absorption bands. DSC and TGA analysis revealed thermal decomposition at 215 °C. Novel gelatin hydrogel (1%, w/v) could withstand a wide range of temperatures, and exhibited high emulsifying activity and viscosity, as well as stable gel clarity from 35 °C to 80 °C. The high temperature treatment (95 °C) produced hydrogel with lower clarity and emulsifying activity but higher viscosity than at the other temperatures. All heat-treated gelatin hydrogels behaved as non-Newtonian fluids as per the Ostwald de Waele model. The novel high α-chain fish skin gelatin has potential broad application in food, pharmaceutical and biological industries.
UR - https://www.scopus.com/pages/publications/85050124546
UR - https://www.scopus.com/inward/citedby.url?scp=85050124546&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2018.07.114
DO - 10.1016/j.ijbiomac.2018.07.114
M3 - Article
C2 - 30031083
AN - SCOPUS:85050124546
SN - 0141-8130
VL - 118
SP - 2278
EP - 2286
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -