Abstract
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.
| Original language | English |
|---|---|
| Journal | Food Hydrocolloids |
| DOIs | |
| Publication status | Accepted/In press - Jan 1 2017 |
| Externally published | Yes |
Fingerprint
Keywords
- Bovine serum albumin
- Cleaning
- Dissolution
- Hydrogel
- Rate limiting
ASJC Scopus subject areas
- Food Science
- Chemistry(all)
- Chemical Engineering(all)
Cite this
Dissolution of bovine serum albumin hydrogels in alkali. / Mercadé-Prieto, Ruben; Coignaud, Maud; Jin, Yuxin; Jeantet, Romain; Chen, Xiao Dong.
In: Food Hydrocolloids, 01.01.2017.Research output: Contribution to journal › Article
}
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
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
UR - http://www.scopus.com/inward/record.url?scp=85035136422&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85035136422&partnerID=8YFLogxK
U2 - 10.1016/j.foodhyd.2017.11.001
DO - 10.1016/j.foodhyd.2017.11.001
M3 - Article
AN - SCOPUS:85035136422
JO - Food Hydrocolloids
JF - Food Hydrocolloids
SN - 0268-005X
ER -