Effect of high hydrostatic pressure on bovine α-lactalbumin functional properties

被引：30

作者：

Octavio Rodiles-Lopez, J. ^{[1
]}

Eugenia Jaramillo-Flores, Ma. ^{[1
]}

Gutierrez-Lopez, Gustavo F. ^{[1
]}

Hernandez-Arana, Andres ^{[2
]}

Fosado-Quiroz, Rosa E. ^{[2
]}

Barbosa-Canovas, Gustavo V. ^{[3
]}

Hernandez-Sanchez, Humberto ^{[1
]}

机构：

[1] Inst Politecn Nacl, Dept Graduados & Invest Alimentos, Escuela Nacl Ciencias Biol, Mexico City, DF, Mexico

[2] Univ Autonoma Metropolitana, Dept Quim, Unidad Iztapalapa, Mexico City, DF, Mexico

[3] Washington State Univ, Dept Biol Syst Engn, Pullman, WA 99164 USA

来源：

JOURNAL OF FOOD ENGINEERING | 2008年 / 87卷 / 03期

关键词：

alpha-lactalbumin; high hydrostatic pressure; functional properties; foaming; solubility;

D O I：

10.1016/j.jfoodeng.2007.12.014

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

The combined effects of high hydrostatic pressure (200, 400 and 600 MPa) and temperature (25, 40 and 55 degrees C) on selected functional properties of alpha-lactalbumin were evaluated in the pH range of 3.0-9.0. Processing at 600 MPa and 55 degrees C for 10 min had a positive effect on solubility, foaming capacity, foam stability, emulsion activity index and emulsion stability of this protein at pH 7. The foaming and emulsifying properties of the protein generally improved by treating its solution at high pressures at all pH values tested, this being in contrast to the reported behavior of pressure treated P-lactoglobulin. Most of the changes in the observed functional properties of pressure treated alpha-lactalbumin solutions were attributed to the modifications brought about in its solubility. (c) 2008 Elsevier Ltd. All rights reserved.

引用

页码：363 / 370

页数：8

共 29 条

[1] Effect of high-pressure treatment on the electrospray ionization mass spectrometry (ESI-MS) profiles of whey proteins [J].

Alvarez, Pedro A. ;

Ramaswamy, Hosahalli S. ;

Ismail, Ashraf A. .

INTERNATIONAL DAIRY JOURNAL, 2007, 17 (08) :881-888

[2] Molecular studies of pressure/temperature-induced structural changes in bovine β-lactoglobulin [J].

Aouzelleg, A ;

Bull, LA ;

Price, NC ;

Kelly, SM .

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2004, 84 (05) :398-404

[3]

Arias M, 2000, MILCHWISSENSCHAFT, V55, P191

[4] SOLUBILITY, EMULSIFYING, AND FOAMING PROPERTIES OF RICE BRAN PROTEIN-CONCENTRATES [J].

BERA, MB ;

MUKHERJEE, RK .

JOURNAL OF FOOD SCIENCE, 1989, 54 (01) :142-145

[5] Functional properties of whey proteins as affected by dynamic high-pressure treatment [J].

Bouaouina, H ;

Desrumaux, A ;

Loisel, C ;

Legrand, J .

INTERNATIONAL DAIRY JOURNAL, 2006, 16 (04) :275-284

[6]

Boyer R., 2000, MODERN EXPT BIOCH

[7] Emulsifying properties of α-lactalbumin after high-pressure treatment and subsequent lactosylation [J].

Bravo, F. I. ;

Villamiel, M. ;

Molina, E. .

HIGH PRESSURE RESEARCH, 2007, 27 (01) :115-119

[8] Effect of high-pressure processing on myofibrillar protein structure [J].

Chapleau, N ;

Mangavel, C ;

Compoint, JP ;

Lamballerie-Anton, MD .

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2004, 84 (01) :66-74

[9] Adsorption dynamics and interfacial properties of α-lactalbumin in native and molten globule state conformation at air-water interface [J].

Cornec, M ;

Kim, DA ;

Narsimhan, G .

FOOD HYDROCOLLOIDS, 2001, 15 (03) :303-313

[10] High pressure effects on emulsifying behavior of whey protein concentrate [J].

Galazka, VB ;

Ledward, DA ;

Dickinson, E ;

Langley, KR .

JOURNAL OF FOOD SCIENCE, 1995, 60 (06) :1341-1343

← 1 2 3 →