Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins

被引：8

作者：

Gaspard, Sophie J. ^{[1
,2
]}

Sunds, Anne, V ^{[3
]}

Larsen, Lotte B. ^{[3
]}

Poulsen, Nina A. ^{[3
]}

O'Mahony, James A. ^{[2
]}

Kelly, Alan L. ^{[2
]}

Brodkorb, Andre ^{[1
]}

机构：

[1] TEAGASC, Food Res Ctr, Moorepk, Cork P61 C996, Ireland

[2] Univ Coll Cork, Sch Food & Nutr Sci, Cork T12 YN60, Ireland

[3] Aarhus Univ, Fac Tech Sci, Dept Food Sci, DK-8200 Aarhus N, Denmark

来源：

JOURNAL OF DAIRY SCIENCE | 2020年 / 103卷 / 06期

关键词：

caseinomacropeptide; sialic acid; whey protein; denaturation; aggregation; HEAT-INDUCED AGGREGATION; BETA-LACTOGLOBULIN; THERMAL-DENATURATION; KAPPA-CASEIN; ALPHA-LACTALBUMIN; MILK; PH; STABILITY; MECHANISM; KINETICS;

D O I：

10.3168/jds.2019-17780

中图分类号：

S8 [畜牧、动物医学、狩猎、蚕、蜂];

学科分类号：

0905 ;

摘要：

The effect of the addition of caseinomacropeptide (CMP) or desialylated CMP on the heat-induced denaturation and aggregation of whey proteins was investigated in the pH range 3 to 7 after heating at 80 degrees C for 30 min. The rate and temperature of denaturation, the extent of aggregation, and the changes in secondary structure of the whey proteins heated in presence of CMP or desialylated CMP were measured. The sialic acid bound to CMP favored the denaturation and aggregation of whey proteins when the whey proteins were oppositely charged to CMP at pH 4. A transition occurred at pH 6, below which the removal of sialic acid enhanced the stabilizing properties of CMP against the denaturation and aggregation of the whey proteins. At pH >6, the interactions between desialylated CMP and the whey proteins led to more extensive denaturation and aggregation. Sialic acid bound to CMP influenced the denaturation and aggregation behavior of whey proteins in a pH-dependent manner, and this should be considered in future studies on the heat stability of such systems containing CMP.

引用

页码：4975 / 4990

页数：16

共 49 条

[1] Thermal stabilization of beta-lactoglobulin by whey peptide fractions [J].

Barbeau, J ;

Gauthier, SF ;

Pouliot, Y .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1996, 44 (12) :3939-3945

[2] Infrared spectroscopy of proteins [J].

Barth, Andreas .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2007, 1767 (09) :1073-1101

[3]

BEYER HJ, 1989, GIT SUPPL LEBENSMITT, V2, P22

[4]

Brody EP, 2000, BRIT J NUTR, V84, pS39, DOI 10.1017/S0007114500002233

[5] Effect of κ-casein deglycosylation on the acid coagulability of milk [J].

Cases, E ;

Vidal, V ;

Cuq, JL .

JOURNAL OF FOOD SCIENCE, 2003, 68 (08) :2406-2410

[6] Caseinomacropeptide modifies the heat-induced denaturatione-aggregation process of β-lactoglobulin [J].

Croguennec, Thomas ;

Leng, Ning ;

Hamon, Pascaline ;

Rousseau, Florence ;

Jeantet, Romain ;

Bouhallab, Said .

INTERNATIONAL DAIRY JOURNAL, 2014, 36 (01) :55-64

[7]

Deeth H. C., 2018, Whey proteins: From milk to medicine

[8]

DOI H, 1981, AGR BIOL CHEM TOKYO, V45, P2351, DOI 10.1080/00021369.1981.10864885

[9] NOMENCLATURE OF PROTEINS OF COWS MILK - 5TH REVISION [J].

EIGEL, WN ;

BUTLER, JE ;

ERNSTROM, CA ;

FARRELL, HM ;

HARWALKAR, VR ;

JENNESS, R ;

WHITNEY, RM .

JOURNAL OF DAIRY SCIENCE, 1984, 67 (08) :1599-1631

[10] Heat-induced aggregation of whey proteins in the presence of κ-casein or sodium caseinate [J].

Guyomarc'h, Fanny ;

Nono, Merveille ;

Nicolai, Taco ;

Durand, Dominique .

FOOD HYDROCOLLOIDS, 2009, 23 (04) :1103-1110

← 1 2 3 4 5 →