29 results match your criteria: "Key Laboratory of Dairy Science Northeast Agricultural University[Affiliation]"
Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate.
Food Chem
March 2020
Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, Harbin 150030, PR China. Electronic address:
Impacts of superfine grinding treatment (0, 2, 4, 6, 8 or 10 h) on structure, physicochemical and rheological properties of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) were investigated. Size exclusion chromatography showed that high molecular weight polymers were formed in TGase-treated sWPI (WPI treated with superfine grinding), whereas its consumption of free amino groups reached the maximum at grinding 8 h and 10 h. With the milling time extended from 0 to 10 h, particle size of the TGase-crosslinked sWPI gradually increased.
View Article and Find Full Text PDFSurface Hydrophobicity and Functional Properties of Citric Acid Cross-Linked Whey Protein Isolate: The Impact of pH and Concentration of Citric Acid.
Molecules
September 2018
Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, Harbin 150030, China.
The effects of citric acid-mediated cross-linking under non-acidic conditions on the surface hydrophobicity, solubility, emulsifying, and foaming properties of whey protein isolate (WPI) were investigated. In this research, citric acid-mediated cross-linking could not only increase the surface hydrophobicity of whey proteins at pH 7.0 and 8.
View Article and Find Full Text PDFCharacterization and comparison of the structure and antioxidant activity of glycosylated whey peptides from two pathways.
Food Chem
August 2018
Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, Harbin 150030, PR China; Inner Mongolia Mengniu Dairy Group Co. Ltd., Hohhot 011517, PR China. Electronic address:
Glycosylated whey peptides (WPP-Gal A and WPP-Gal B) were formed from two pathways. WPP-Gal A showed higher browning intensity and fluorescence intensity than WPP-Gal B. Loss of amino groups and reducing sugar was heavier for WPP-Gal A than WPP-Gal B.
View Article and Find Full Text PDFEffects of ultrasound treatment on physico-chemical, functional properties and antioxidant activity of whey protein isolate in the presence of calcium lactate.
J Sci Food Agric
March 2018
Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, College of Food Science and Technology, Harbin, P.R. China.
Background: The aim of this study was to investigate the effects of ultrasound applied at various powers (0, 200, 400, 600 or 800 W) and for different times (20 or 40 min) on the physico-chemical, functional properties and antioxidant activities of whey protein isolate (WPI) dispersions in the presence of 1.20 mmol L calcium lactate.
Results: Surface hydrophobicity and free sulfhydryl group of the WPI dispersions containing 1.