共 60 条
Changes in structure and antioxidant activity of β-lactoglobulin by ultrasound and enzymatic treatment
被引:63
作者:
Ma, Shuang
[1
]
Wang, Cuina
[1
]
Guo, Mingruo
[1
,2
,3
]
机构:
[1] Jilin Univ, Coll Food Sci & Engn, Dept Food Sci, Changchun 130062, Jilin, Peoples R China
[2] Univ Vermont, Coll Agr & Life Sci, Dept Nutr & Food Sci, Burlington, VT 05405 USA
[3] Northeast Agr Univ, Dept Food Sci, Harbin 150030, Heilongjiang, Peoples R China
关键词:
beta-Lactoglobulin;
Ultrasound treatment;
Proteolysis;
Antioxidant activity;
HIGH-INTENSITY-ULTRASOUND;
WHEY PROTEINS;
EMULSIFYING PROPERTIES;
PEPTIDE FRACTIONS;
FLUORESCENT-PROBE;
HIGH-PRESSURE;
IN-VITRO;
HYDROLYSIS;
MILK;
BINDING;
D O I:
10.1016/j.ultsonch.2018.01.017
中图分类号:
O42 [声学];
学科分类号:
070206 ;
082403 ;
摘要:
Effects of ultrasound (20-40% amplitudes at 45-55 degrees C) and enzymatic (pepsin and trypsin) treatment on structure and antioxidant activity of beta-lactoglobulin were studied. Changes in structure of beta-lactoglobulin were investigated using spectroscopy techniques and changes in antioxidant activity were measured by chemical and cellular-based assays. Ultrasound treatment had considerable impact on the structure of beta-lactoglobulin and increased the susceptibility of beta-actoglobulin to both pepsin and trypsin proteolysis. Intrinsic fluorescence intensity of beta-lactoglobulin was increased by ultrasound and then decreased after following enzymatic treatment. Compared with control, the beta-lactoglobulin after ultrasound and enzymatic treatments showed significantly higher oxygen scavenging activities in Caco-2 cells models, ABTS (2, 2'-Azinobis-3-ethylbenzthiazoline-6-sulphonate) radical scavenging activity and oxygen radical absorbance capacity (p < 0.05). Results indicated that ultrasound treatment increased the proteolysis of fl-lactoglobulin by both pepsin and trypsin and improved the antioxidant activity of the protein and its proteolytic products.
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页码:227 / 236
页数:10
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