KINETICS and MECHANISM of NONENZYMATIC DEAMIDATION of SOY PROTEIN

JIB ZHANG; TUNG CHING LEE; CHI‐TANG ‐T HO

doi:10.1111/j.1745-4549.1993.tb00730.x

KINETICS and MECHANISM of NONENZYMATIC DEAMIDATION of SOY PROTEIN

JIB ZHANG, TUNG CHING LEE, CHI‐TANG ‐T HO

School of Environmental and Biological Sciences, Food Science

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Nonenzymatic deamidation of glutamine and asparagine residues of soy protein in aqueous solutions of varying pH (3.0, 5.0, 7.0, 9.0 and 11.0) at different temperatures (100C, 115C and 130C) was monitored over a period of time. the deamidation of soy protein followed first‐order kinetics. the activation energies (Ea) of soy protein deamidation at different pHs ranged from 14 to 27 Kcal/mol. the activation energies were highly pH‐dependent and decreased very sharply as the pH went up from pH 5 to pH 11.

Original language	English (US)
Pages (from-to)	259-268
Number of pages	10
Journal	Journal of Food Processing and Preservation
Volume	17
Issue number	4
DOIs	https://doi.org/10.1111/j.1745-4549.1993.tb00730.x
State	Published - Aug 1993

All Science Journal Classification (ASJC) codes

Food Science
General Chemistry
General Chemical Engineering

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title = "KINETICS and MECHANISM of NONENZYMATIC DEAMIDATION of SOY PROTEIN",

abstract = "Nonenzymatic deamidation of glutamine and asparagine residues of soy protein in aqueous solutions of varying pH (3.0, 5.0, 7.0, 9.0 and 11.0) at different temperatures (100C, 115C and 130C) was monitored over a period of time. the deamidation of soy protein followed first‐order kinetics. the activation energies (Ea) of soy protein deamidation at different pHs ranged from 14 to 27 Kcal/mol. the activation energies were highly pH‐dependent and decreased very sharply as the pH went up from pH 5 to pH 11.",

author = "JIB ZHANG and LEE, {TUNG CHING} and HO, {CHI‐TANG ‐T}",

year = "1993",

month = aug,

doi = "10.1111/j.1745-4549.1993.tb00730.x",

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journal = "Journal of Food Processing and Preservation",

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AU - LEE, TUNG CHING

AU - HO, CHI‐TANG ‐T

PY - 1993/8

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N2 - Nonenzymatic deamidation of glutamine and asparagine residues of soy protein in aqueous solutions of varying pH (3.0, 5.0, 7.0, 9.0 and 11.0) at different temperatures (100C, 115C and 130C) was monitored over a period of time. the deamidation of soy protein followed first‐order kinetics. the activation energies (Ea) of soy protein deamidation at different pHs ranged from 14 to 27 Kcal/mol. the activation energies were highly pH‐dependent and decreased very sharply as the pH went up from pH 5 to pH 11.

AB - Nonenzymatic deamidation of glutamine and asparagine residues of soy protein in aqueous solutions of varying pH (3.0, 5.0, 7.0, 9.0 and 11.0) at different temperatures (100C, 115C and 130C) was monitored over a period of time. the deamidation of soy protein followed first‐order kinetics. the activation energies (Ea) of soy protein deamidation at different pHs ranged from 14 to 27 Kcal/mol. the activation energies were highly pH‐dependent and decreased very sharply as the pH went up from pH 5 to pH 11.

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KINETICS and MECHANISM of NONENZYMATIC DEAMIDATION of SOY PROTEIN

Abstract

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