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

[Display omitted] •Conversion of large-scale waste whey into value-added food products.•Fermentation led to the improvement in solubility, emulsifying properties of FWPC.•Modified FWPCs resulted in improved functional and physicochemical properties.•Sequentially treated FWPCs are proposed for enhanc...

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Published in:Food research international 2023-01, Vol.163, p.112158-112158, Article 112158
Main Authors: Gantumur, Munkh-Amgalan, Hussain, Muhammad, Li, Jinzhe, Hui, Mizhou, Bai, Xi, Sukhbaatar, Narantuya, Li, Jinpeng, Chen, Wei, Hou, Juncai, Jiang, Zhanmei
Format: Article
Language:English
Subjects:
Cross-linking
Fermentation
Fermented whey protein
Polymers
Protein Structure, Secondary
Recovery
Solubility
Transglutaminases - metabolism
Ultrasound
Whey
Whey Proteins - chemistry
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Summary:[Display omitted] •Conversion of large-scale waste whey into value-added food products.•Fermentation led to the improvement in solubility, emulsifying properties of FWPC.•Modified FWPCs resulted in improved functional and physicochemical properties.•Sequentially treated FWPCs are proposed for enhanced food-grade protein production. 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 
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2022.112158