Effect of Keratinase Modification on the Foaming Properties and Structural Characteristics of Rice Protein Hydrolysate

Xiaojiang WU; Huoyan TONG; Yin WAN; Guiming FU; Chengmei LIU

doi:10.13386/j.issn1002-0306.2020060186

Volume 42 Issue 8

Apr. 2021

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Science and Technology of Food Industry > 2021 > 42(8): 29-35. > DOI: 10.13386/j.issn1002-0306.2020060186

WU Xiaojiang, TONG Huoyan, WAN Yin, et al. Effect of Keratinase Modification on the Foaming Properties and Structural Characteristics of Rice Protein Hydrolysate[J]. Science and Technology of Food Industry, 2021, 42(8): 29−35. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2020060186.

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Effect of Keratinase Modification on the Foaming Properties and Structural Characteristics of Rice Protein Hydrolysate

State Key Laboratory of Food Science and Technology, College of Food Science and Technology, Nanchang University, Nanchang 330031, China

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Received Date: June 14, 2020
Available Online: February 01, 2021

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Abstract

Abstract

In this study, rice protein (RP) was hydrolyzed by keratinase, and partial functional properties (foaming properties, amino acid composition) and structural characteristics including SDS-PAGE, circular dichroism, and endogenous fluorescence of RP hydrolysate (RPH) with different degree of hydrolysis(DH) were determined. Results showed that the protein recovery rate of RP under neutral conditions was significantly improved by keratinase (P < 0.05). The foamability of RPH showed a trend of increasing first and then decreasing with the increase of DH. And there was no significant change in foaming stability among RPH. The contents of sweet amino acid, umami amino acid in RPH were significantly higher (P < 0.05) compared with RP without hydrolysis. The result of SDS-PAGE showed that RPH was mainly composed of polypeptides with a molecular weight of less than 20 kDa. There was significant increase in the proportion of random coils and significant decrease in the proportion of α-helix and β-fold in the secondary structure of RPH than those in RP without hydrolysis (P < 0.05), indicating that the secondary structure in RPH got more flexible and looser than that in RP without hydrolysis. The endogenous fluorescence results indicated that more contents of hydrophobic amino acids exposed in water phase after hydrolysis. This study would provide a theoretical basis for the development and utilization of RP products.
- rice protein,
- keratinase,
- protein recovery rate,
- protein structure

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