TY - JOUR
T1 - Dissolution of bovine serum albumin hydrogels in alkali
AU - Mercadé-Prieto, Ruben
AU - Coignaud, Maud
AU - Jin, Yuxin
AU - Jeantet, Romain
AU - Chen, Xiao Dong
N1 - Funding Information:
This work was supported by the project funding from the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD) and the “Jiangsu Specially-Appointed Professors Program” of China , the Youth Fund of Natural Science Foundation of Jiangsu Province of China (No. BK20140343 ), and the National Natural Science Foundation of China , International Cooperation and Exchange Program (No. 21550110192 ).
PY - 2017/1/1
Y1 - 2017/1/1
N2 - Heat-induced protein gelled deposits, occurring during dairy processing, are industrially cleaned with caustic-based solutions. In order to develop general dissolution mechanisms of protein hydrogels, in analogy to general gelation mechanisms for globular proteins, different protein systems must be characterized. We report the first characterization of the dissolution behaviour of heat-set pure bovine serum albumin (BSA) hydrogels. At low alkali concentrations (<0.2 M NaOH), the formed BSA gels were dissolved as observed for whey protein mixtures or pure β-lactoglobulin gels. The key rate limiting step is suggested to be the destruction of inter-protein non-covalent interactions. At higher NaOH concentrations (>0.2 M) the dissolution rate of BSA gels was fairly constant, unlike seen before. Activation energy estimations of the rate yield very low value in certain conditions, again unlike seen before. It is suggested that mass transfer limitations occur during dissolution due to the large BSA size.
AB - Heat-induced protein gelled deposits, occurring during dairy processing, are industrially cleaned with caustic-based solutions. In order to develop general dissolution mechanisms of protein hydrogels, in analogy to general gelation mechanisms for globular proteins, different protein systems must be characterized. We report the first characterization of the dissolution behaviour of heat-set pure bovine serum albumin (BSA) hydrogels. At low alkali concentrations (<0.2 M NaOH), the formed BSA gels were dissolved as observed for whey protein mixtures or pure β-lactoglobulin gels. The key rate limiting step is suggested to be the destruction of inter-protein non-covalent interactions. At higher NaOH concentrations (>0.2 M) the dissolution rate of BSA gels was fairly constant, unlike seen before. Activation energy estimations of the rate yield very low value in certain conditions, again unlike seen before. It is suggested that mass transfer limitations occur during dissolution due to the large BSA size.
KW - Bovine serum albumin
KW - Cleaning
KW - Dissolution
KW - Hydrogel
KW - Rate limiting
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U2 - 10.1016/j.foodhyd.2017.11.001
DO - 10.1016/j.foodhyd.2017.11.001
M3 - Article
AN - SCOPUS:85035136422
VL - 77
SP - 598
EP - 606
JO - Food Hydrocolloids
JF - Food Hydrocolloids
SN - 0268-005X
ER -