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Covalent Crosslinking in Heated Protein Systems
Author(s) -
Mohammed Z.H.,
Hill S.E.,
Mitchell J.R.
Publication year - 2000
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2000.tb15983.x
Subject(s) - solubility , isoelectric point , chemistry , bovine serum albumin , chromatography , egg white , browning , covalent bond , gelatin , whey protein , sodium , sodium dodecyl sulfate , casein , sodium caseinate , food science , organic chemistry , enzyme
Changes in the solubility (in water or in 1% sodium dodecyl sulfate plus 1%β‐mercaptoethanol), isoelectric point, and degree of browning were followed for a range of food proteins when they were heated to 105 to 145°C at 3 relative humidities (RH). In general, there is a decrease in solubility with increasing RH and temperature of heating, but most proteins also showed an increase in solubility on extensive heating. The order for the proteins, based on the temperatures at which an increase in solubility occurred was: gelatin < gluten < soya isolate, sodium caseinate < egg albumin, bovine serum albumin < whey isolate, milk powder, β‐lactoglobulin. The bonds that could be formed and broken during this thermal treatment are considered.