Abstract

Rice bran protein (RBP) hydrolysis was conducted after high hydrostatic pressure (HHP) pretreatment. The structural and functional properties of HHP-pretreated rice bran protein hydrolysates (RBPH) were investigated. HHP pretreatments were conducted at 100, 200, and 300 MPa; then, enzymatic hydrolysis at atmospheric pressure was performed using trypsin. An RBPH sample that had not been pretreated by HHP was used as a control. Free sulfhydryl (SH) content, SDS-PAGE profiles, high-performance size exclusion chromatography (HPSEC), Fourier transform infrared (FTIR) spectrum, scanning electron microscopy (SEM), intrinsic fluorescence spectrum, solubility, and emulsifying and foaming properties were evaluated. Changes in particle size and ζ-potential were monitored. Compared with the control, the results of solubility, the emulsifying activity index (EAI) and the emulsifying stability index (ESI) increased significantly (p < 0.05) at 200 MPa. The content of free SH increased significantly (p < 0.05) at 100 MPa. FTIR spectrum and fluorescence analysis confirmed the changes in the secondary and tertiary structures. The experimental results indicated that the structural and functional properties of HHP-pretreated RBPH improved.

Highlights

  • Rice bran is a low-priced, underutilized major by-product of rice processing [1]

  • The current work indicated that rice bran protein hydrolysates (RBPH) exhibited significant improvements over the control in terms of the solubility, emulsifying properties, and foaming properties

  • The findings may indicate that high hydrostatic pressure (HHP) changed the spatial structure of Rice bran protein (RBP), enhancing the efficiency and effect of hydrolysis

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Summary

Introduction

Rice bran contains protein (12–16%), fat (15–20%), and fiber (23–28%) [2]. It contains many other nutrients, such as phytosterols, vitamins, and antioxidants [3]. Rice bran protein (RBP), which contains lysine (3–4%), is a high-quality resource of protein for the food processing industry, and the content of lysine in RBP is much higher than that of proteins from many other cereal brans or legumes [4,5]. RBP is used in the modern infant food industry because it is a low-allergy protein [6,7]. Low solubility limits the application of natural RBP owing to the disulfide bonds and hydrophobic interactions in RBP, which control the spatial structure of protein [10,11]. Proper methods of modification are required to obtain suitable functional and structural protein properties

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