Modulation of physico-chemical properties of bovine β-casein by nonenzymatic glycation associated with enzymatic dephosphorylation

被引：12

作者：

Darewicz, M ^{[1
]}

Dziuba, J ^{[1
]}

Mioduszewska, H ^{[1
]}

Minkiewicz, P ^{[1
]}

机构：

[1] Olsztyn Univ Agr & Technol, Dept Food Biochem, PL-10726 Olsztyn Kortowo, Poland

来源：

ACTA ALIMENTARIA | 1999年 / 28卷 / 04期

关键词：

beta-casein; dephosphorylation; glycation; solubility; stabilization ability;

D O I：

10.1556/AAlim.28.1999.4.5

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

A major bovine casein fraction, beta-casein was chemically glycated and/or enzymatically dephosphorylated. Ten glucose and nine lactose moieties were attached while all phosphate groups were removed. Glycation shifted the pl to acidic pH range and decreased the solubility at acidic pHs while dephosphorylation shifted the pl to neutral pH range and increased the solubility at acidic pHs. Dephosphorylation led to longer retention time measured using the reversed-phase high-performance liquid chromatography and affected UV-spectra of beta-casein which suggested structural changes. Glycation did not affect these properties. Both modifications decreased the calcium sensitivity of beta-casein, making it to keep alpha(S1)-casein in solution in the presence of Ca2+.

引用

页码：339 / 354

页数：16

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