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Thermal stability improvement of rice bran albumin protein incorporated with epigallocatechin gallate
journal contributionposted on 2018-03-09, 00:00 authored by Z Zhou, J Xu, Y Liu, D Meng, X Sun, H Yi, Y Gao, G Sun, Padraig Strappe, C Blanchard
Rice bran albumin protein (RAP) is sensitive to thermal changes and tends to degrade when exposed to high-temperature processing. In this work, RAP–epigallocatechin-3-gallate (EGCG) complex (RAPE) was prepared and the thermal stability was evaluated. Fluorescence results showed that EGCG could interact with RAP with a binding number n of 0.0885:1 (EGCG:RAP, w/w) and a binding constant K of 1.02 (± 0.002) ×104/M, suggesting both hydrogen bonding and van der Waals forces played an important role. FTIR analysis demonstrated that EGCG could induce secondary structural changes in RAP above a ratio of 1.6:1 (EGCG:RAP, w/w). Interestingly, the secondary structure changes of RAPE at different temperatures (25, 50, 60, 70, and 80 °C) were inhibited compared with that for RAP, suggesting RAPE was more resistant and stable to the heat treatment. In addition, a dense porous structure of RAPE was achieved due to the EGCG binding after thermal treatment. Furthermore, the Tpeak temperature of RAPE increased significantly from 64.58 to 74.16 °C and the enthalpy also increased from 85.53 to 138.52 J/g with a mass ratio increasing from 0 to 3.2 (EGCG:RAP, w/w), demonstrating the thermal stability of RAPE. In addition, the valine, methionine, and lysine content in RAPE were significantly higher than RAP following 80 °C treatment for 20 min (P < 0.05), exhibiting enhanced amino acid profiles, which might be due to EGCG–RAP interactions and microenvironment changes around relevant amino acids. These findings demonstrate that EGCG has the potential to improve the thermal stability of sensitive proteins and is beneficial for usage in the food industry.
Number of Pages8
External Author AffiliationsTianjin Univ. of Science and Technology, China; Tianjin Food Safety & Low Carbon Manufacturing Collaborative Innovation Center, China