Modification of fermented whey protein concentrates: Impact of sequential ultrasound and TGase cross-linking

Munkh-Amgalan Gantumur; Muhammad Hussain; Jinzhe Li; Mizhou Hui; Xi Bai; Narantuya Sukhbaatar; Jinpeng Li; Wei Chen; Juncai Hou; Zhanmei Jiang

doi:10.1016/j.foodres.2022.112158

Modification of fermented whey protein concentrates: Impact of sequential ultrasound and TGase cross-linking

Food Res Int. 2023 Jan:163:112158. doi: 10.1016/j.foodres.2022.112158. Epub 2022 Nov 19.

Authors

Affiliations

¹ Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, PR China; College of Life Sciences, Northeast Agricultural University, Harbin 150030, PR China.
² Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, PR China.
³ College of Life Sciences, Northeast Agricultural University, Harbin 150030, PR China; Frontier Biotechnology Laboratory, Hangzhou International Innovation Center, Zhejiang University, Hangzhou, 311200, PR China.
⁴ College of Life Sciences, Northeast Agricultural University, Harbin 150030, PR China.
⁵ School of Industrial Technology, Mongolian University of Science and Technology, 14191, Baga toiruu 34, Sukhbaatar district Ulaanbaatar, Mongolia.
⁶ Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, PR China. Electronic address: jchou@neau.edu.cn.
⁷ Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, PR China. Electronic address: zhanmeijiang@neau.edu.cn.

PMID: 36596109
DOI: 10.1016/j.foodres.2022.112158

Abstract

This study aimed to examine the impact of fermentation process on whey protein and improve the general properties of fermented whey protein concentrate (FWPC) recovered by a combined ultrafiltration-diafiltration (UF-DF) operation. Impacts of sequential ultrasound (US) pretreatment and transglutaminase (TGase) crosslinking on structural, functional, and physicochemical properties of FWPCs were investigated. Partially denatured and hydrolyzed fermented whey protein could replace heat denaturation prior to the TGase addition to a whey protein system. Sequential treatment increased the molecular weight of FWPCs as exhibited by both SEM and SDS-PAGE, which demonstrates that modification can lead to the polymers and oligomers production. The zeta potential value increased significantly after US treatment and enzyme catalysis, and all the modified FWPCs were strongly negatively charged. Compared with the secondary structure of untreated FWPCs, the percentage of α-helix and random coil in modified FWPCs significantly increased, while the percentage of β-sheet and β-turns reduced. Solubility, free sulfhydryl groups, and surface hydrophobicity of all FWPCs were significantly improved compared to non-fermented WPC (P < 0.05). Sequential treatment induced a substantial impact on the emulsifying activity and stability of modified samples in comparison with untreated FWPCs. Scanning electron microscope pictures confirmed the positive effects of sequential treatments on texture and void size reduction. Therefore, the application of recovering modified FWPCs is fully recommended as a commercially viable approach for enhanced protein production at the industrial scale.

Keywords: Cross-linking; Fermentation; Fermented whey protein; Recovery; Ultrasound; Whey.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Polymers*
Protein Structure, Secondary
Solubility
Transglutaminases* / metabolism
Whey Proteins / chemistry

Substances

Whey Proteins
Transglutaminases
Polymers