Influence of hydrolysis temperature and pH on the selective hydrolysis of whey proteins by trypsin and potential recovery of native alpha-lactalbumin

被引：41

作者：

Cheison, Seronei C. ^{[1
,2
]}

Leeb, Elena ^{[1
]}

Toro-Sierra, Jose ^{[3
,4
]}

Kulozik, Ulrich ^{[3
,4
]}

机构：

[1] Tech Univ Munich, Zent Inst Ernahrungs & Lebensmittel Forsch ZIEL, Jr Res Grp Bioact Peptides & Prot Technol, D-85354 Freising Weihenstephan, Germany

[2] Maseno Univ, Sch Publ Hlth & Community Dev, Kisumu, Kenya

[3] Tech Univ Munich, Chair Food Proc Engn, D-85354 Freising Weihenstephan, Germany

[4] Tech Univ Munich, Dairy Technol Dept, ZIEL Technol Sect, D-85354 Freising Weihenstephan, Germany

来源：

INTERNATIONAL DAIRY JOURNAL | 2011年 / 21卷 / 03期

关键词：

BOVINE BETA-LACTOGLOBULIN; THERMAL-TREATMENT; MEMBRANE; FRACTIONATION; SEPARATION; OPTIMIZATION; ENZYMES;

D O I：

10.1016/j.idairyj.2010.09.008

中图分类号：

TS2 [食品工业];

学科分类号：

100403 [营养与食品卫生学];

摘要：

Whey protein isolate (93.84% protein) was hydrolysed using bovine trypsin (EC 3.4.21.4) at an enzyme-to-substrate ratio of 1.0% (w w(-1)) over a range of temperatures and pH. Residual protein was quantified using reversed-phase high performance liquid chromatography. Genetic variants A and B of beta-lactoglobulin (beta-Lg) and alpha-lactalbumin (alpha-La) showed higher resistance to trypsin hydrolysis at 25 degrees C than at 50 degrees C with higher susceptibility of beta-LgA than of beta-LgB. Under the conditions trialled, the highest (67.87%) residual pure alpha-La was at 25 degrees C and pH 8.5 (2 h hydrolysis; degree of hydrolysis 7.11%), while the lowest (7.99%) was at 50 degrees C, pH 8.5 (5 min). Above pH 7.5 and 40 degrees C, beta-Lg dimer-monomer transition occurred resulting in improved trypsin hydrolysis. Trypsin hydrolysis outside the optimum pH and temperature offers potential for selective removal of beta-LgAnd production of pure and native alpha-La. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：166 / 171

页数：6

共 27 条

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[2]

Separation and characterization of β-lactoglobulin and α-lactalbumin from whey and whey protein preparations [J].