Dissolution of bovine serum albumin hydrogels in alkali

Ruben Mercadé-Prieto, Maud Coignaud, Yuxin Jin, Romain Jeantet, Xiao Dong Chen

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 languageEnglish
JournalFood Hydrocolloids
DOIs
Publication statusAccepted/In press - Jan 1 2017
Externally publishedYes

Fingerprint

Hydrogels
hydrocolloids
Alkalies
bovine serum albumin
Bovine Serum Albumin
alkalis
Dissolution
Proteins
proteins
Hot Temperature
heat
Caustics
Dairies
Gelation
gelation
activation energy
mass transfer
dairies
Mass transfer
Deposits

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 journalArticle

Mercadé-Prieto, Ruben ; Coignaud, Maud ; Jin, Yuxin ; Jeantet, Romain ; Chen, Xiao Dong. / Dissolution of bovine serum albumin hydrogels in alkali. In: Food Hydrocolloids. 2017.
@article{a192b86abc504fe79d4135fb6aa0c183,
title = "Dissolution of bovine serum albumin hydrogels in alkali",
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.",
keywords = "Bovine serum albumin, Cleaning, Dissolution, Hydrogel, Rate limiting",
author = "Ruben Mercad{\'e}-Prieto and Maud Coignaud and Yuxin Jin and Romain Jeantet and Chen, {Xiao Dong}",
year = "2017",
month = "1",
day = "1",
doi = "10.1016/j.foodhyd.2017.11.001",
language = "English",
journal = "Food Hydrocolloids",
issn = "0268-005X",
publisher = "Elsevier",

}

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

JO - Food Hydrocolloids

JF - Food Hydrocolloids

SN - 0268-005X

ER -