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Effect of enzymatic hydrolysis on the formation and structural properties of peanut protein gels

  • Shan Jiang , Junting Zhang , Suhong Li and Chunhong Zhang EMAIL logo
Published/Copyright: November 20, 2020

Abstract

The limited enzymatic hydrolysis gelation method was investigated using peanut protein isolate (PPI) without any coagulators. A peanut protein gel could be formed by enzyme treatment with Alcalase at low temperature (50–70 °C). The influence of enzymatic hydrolysis on the rheological and physicochemical properties was investigated. Structural changes in the PPI were characterized by analyzing the subunits, chemical forces, surface hydrophobicity, fluorescence spectra, and circular dichroism (CD) spectra. The results revealed that enzymatic hydrolysis significantly affected the conarachin II protein of PPI, and had little influence on conarachin I and the basic subunits of arachin. Hydrophobic interaction was the main chemical force active in the peanut protein gel. An increase in the surface hydrophobicity coupled with red-shifts of the fluorescence spectra indicated that inner hydrophobic regions were exposed after hydrolysis, resulting in gel formation via hydrophobic interactions. The CD spectra showed that significant changes occurred in the secondary structure of PPI, where the ordered PPI structure formed a more open structure after enzymatic hydrolysis.


Corresponding author: Chunhong Zhang, College of Food, Shenyang Agricultural University, No. 120 Dongling Road, Shenhe District, Shenyang City 110866, China, E-mail:

Acknowledgments

This work was supported by the Key Laboratory Program of Shenyang, China (Grant No. 17-158-1-00) and the Liaoning Provincial Nature Science Foundation of China (Grant No. 2013020067).

  1. Author contribution: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: None declared.

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Received: 2018-10-19
Accepted: 2020-11-06
Published Online: 2020-11-20

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