Effects of Different Thermal Sterilization Conditions on Structural and Functional Properties of Whey and Casein Proteins in Goat Milk

被引：0

作者：

Ma, Yutong ^{[1
]}

Qiao, Ziyan ^{[1
]}

Zeng, Qingkun ^{[2
]}

Yang, Pan ^{[2
]}

Li, Ling ^{[2
]}

Chen, Lin ^{[1
]}

Feng, Xianchao ^{[1
]}

机构：

[1] College of Food Science and Engineering, Northwest A&F University, Yangling

[2] Guangxi Zhuang Autonomous Region Buffalo Research Institute, Nanning

来源：

Shipin Kexue/Food Science | 2024年 / 45卷 / 15期

关键词：

casein; functional features; goat milk; structural properties; whey protein;

D O I：

10.7506/spkx1002-6630-20231122-165

中图分类号：

学科分类号：

摘要：

This study investigated the effects of different thermal sterilization conditions on the structural and functional properties of whey and caseins in goat milk. The commonly used industrial sterilization conditions including 65 ℃ for 30 min, 80 ℃ for 30 s, 95 ℃ for 5 min and 135 ℃ for 4 s were selected to treat goat milk, and whey and casein proteins were separated from the treated milk. Circular dichroism (CD) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy, laser confocal scanning microscopy (LCSM) and atomic force microscopy (AFM) were used to analyze the changes in protein structure and properties. The results showed that the structures of whey and casein proteins changed little after treatment at 65 ℃ for 30 min and 80 ℃ for 30 s, and the increase in protein unfolding and surface hydrophobicity resulted in better foaming and emulsifying properties of whey and casein proteins. The treatments at 95 ℃ for 5 min and 135 ℃ for 4 s resulted in a significant decrease in the relative content of α-helix, a significant increase in the relative content of random coil, severe denaturation of the proteins, and a decrease in solubility and surface hydrophobicity, which adversely affected the stability of functional properties of goat milk proteins. The above results provide a reference for optimizing the quality and stability of goat milk products, and help to develop functional goat milk products. © 2024 Chinese Chamber of Commerce. All rights reserved.

引用

页码：67 / 76

页数：9

共 20 条

[1]

PAN Y, XIA Y, YU X X, Et al., Comparative analysis of lipid digestion characteristics in human, bovine, and caprine milk based on simulated in vitro infant gastrointestinal digestion, Journal of Agricultural and Food Chemistry, 69, 35, pp. 10104-10113, (2021)

[2]

CHEN D, LI X Y, ZHAO X, Et al., Comparative proteomics of goat milk during heated processing, Food Chemistry, 275, pp. 504-514, (2019)

[3]

QIN Y S, JIANG H, WANG C F, Et al., Physicochemical and functional properties of goat milk whey protein and casein obtained during different lactation stages, Journal of Dairy Science, 104, 4, pp. 3936-3946, (2021)

[4]

MELINI F, MELINI V, LUZIATELLI F, Et al., Raw and heat-treated milk: from public health risks to nutritional quality, Beverages, 3, 4, (2017)

[5]

SONG B, ZHANG Y M, YANG B J, Et al., Effect of different temperature-controlled ultrasound on the physical and functional properties of micellar casein concentrate, Foods, 10, 11, (2021)

[6]

HAN T L, WANG M Y, WANG Y, Et al., Effects of high-pressure homogenization and ultrasonic treatment on the structure and characteristics of casein, LWT-Food Science and Technology, 130, (2020)

[7]

AKKERMAN M, RAUH V M, CHRISTENSEN M, Et al., Effect of heating strategies on whey protein denaturation-revisited by liquid chromatography quadrupole time-of-flight mass spectrometry, Journal of Dairy Science, 99, 1, pp. 152-166, (2016)

[8]

CALVO M M, LEAVER J, BANKS J M., Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin, International Dairy Journal, 3, 8, pp. 719-727, (1993)

[9]

WIJAYANTI H B, BANSAL N, DEETH H C., Stability of whey proteins during thermal processing: a review, Comprehensive Reviews in Food Science and Food Safety, 13, 6, pp. 1235-1251, (2014)

[10]

GENENE A, HANSEN E B, ESHETU M, Et al., Effect of heat treatment on denaturation of whey protein and resultant rennetability of camel milk, LWT-Food Science and Technology, 101, pp. 404-409, (2019)

← 1 2 →