Covalent crosslinking in heated protein systems

被引：64

作者：

Mohammed, ZH ^{[1
]}

Hill, SE ^{[1
]}

Mitchell, JR ^{[1
]}

机构：

[1] Univ Nottingham, Sch Biol Sci, Div Food Sci, Loughborough LE12 5RD, Leics, England

来源：

JOURNAL OF FOOD SCIENCE | 2000年 / 65卷 / 02期

关键词：

proteins; heat degradation; crosslinking; extrusion;

D O I：

10.1111/j.1365-2621.2000.tb15983.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Changes in the solubility (in water or in 1% sodium dodecyl sulfate plus 1% beta-mercaptoethanol), isoelectric point, and degree of browning were followed for a range of food proteins when they were heated to 105 to 145 degrees 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, beta-lactoglobulin. The bonds that could be formed and broken during this thermal treatment are considered.

引用

页码：221 / 226

页数：6

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