Effects of thermal sterilization on soy protein isolate/polyphenol complexes: Aspects of structure, in vitro digestibility and antioxidant activity. (October 2018)

• Record Type: Journal Article
• Authors: Ren, Cong; Xiong, Wenfei; Peng, Dengfeng; He, Yun; Zhou, Peiyuan; Li, Jing; Li, Bin
• Is Part Of: Food research international. Volume 112(2018)
• Page Start: 284
• Page End: 290
• Publication Date: 2018-10
• Subjects: Soy protein isolate -- Black soybean seed coat extract -- Pasteurization -- High-temperature sterilization; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2018.06.034
• Languages: English
• ISSNs: 0963-9969

Abstract

Abstract: The main purpose of this work was to investigate the influence of typical thermal sterilization approaches (pasteurization, high-temperature sterilization) on the structure, in vitro digestibility, and antioxidant activity of soy protein isolate (SPI)/black soybean seed coat extract (BE) complexes at pH 7.0. The results of zeta potential and particle size demonstrated that the addition of BE was contributed to inhibit protein thermal aggregation. Heat sterilization resulted in protein unfolding revealed by UV–Vis, circular dichroism, and fluorescence spectroscopy analysis. The increase of BE led to the reduction of fluorescence intensity and surface hydrophobicity of SPI. Moreover, the formation of SPI/BE complexes inhibited protein digestion in vitro, while thermal sterilization promoted protein digestion. The SPI/BE complexes showed a strong radical scavenging ability both before and after thermal treatment. Graphical abstract: Highlights: The influence of typical thermal sterilization on SPI/BE complexes was investigated. The formation of SPI/BE complexes inhibited the aggregation of SPI during heating. Thermal sterilization accelerated protein digestibility in vitro, while BE inhibited it. Thermal sterilization had little effect on the antioxidant activity of SPI/BE complexes.