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大米蛋白水解物作为一种水包油型乳液稳定剂的性能。

Performance of rice protein hydrolysates as a stabilizing agent on oil-in-water emulsions.

机构信息

Department of Food Engineering and Technology, School of Food Engineering, University of Campinas, 13083-862 Campinas, SP, Brazil.

Department of Food Engineering and Technology, School of Food Engineering, University of Campinas, 13083-862 Campinas, SP, Brazil.

出版信息

Food Res Int. 2023 Oct;172:113099. doi: 10.1016/j.foodres.2023.113099. Epub 2023 Jun 15.

Abstract

Rice protein isolate (RPI) has been receiving increasing attention from the food industry due to its performance as an emulsifier. However, it is possible to enlarge its field of applications through enzymatic hydrolysis. Therefore, this work aimed to investigate the effects of the controlled enzymatic hydrolysis (degree of hydrolysis DH as 2, 6, and 10%) using Flavourzyme on the physicochemical properties of rice protein and to identify the minimum concentration of these hydrolysates (0.5, 1.0, and 1.5%) to form and stabilize oil/water emulsion. The physicochemical, interfacial tension (IT), and surface characteristics of RPI and their hydrolysates (RPH) were determined. Even at a lower protein concentration (1.0%), protein hydrolysate presented lower IT when compared with RPI at a higher protein concentration (1.5%). The interfacial tension decreased from 17.6 mN/m to 9.9 mN/m when RPI was hydrolyzed. Moreover, enzymatic hydrolysis (DH 6 and 10%) enhanced the protein solubility by almost 20% over a pH range of 3-11. The improved amphiphilic property of RPH, supported by the results of IT and solubility, was confirmed by the higher emulsion stability indicated by the Turbiscan and emulsion stability indexes. Emulsions stabilized by RPH (DH 6% and 10%) at lower protein concentrations (1%) exhibited better physical stability than RPI at higher protein concentrations (1.5%). In this work, we verified the minimum concentration of rice protein hydrolysate required to form and stabilize oil-in-water (O/W) emulsions.

摘要

米蛋白分离物(RPI)由于其作为乳化剂的性能而受到食品工业的越来越多的关注。然而,通过酶水解可以扩大其应用领域。因此,本工作旨在研究使用 Flavourzyme 对米蛋白的可控酶水解(水解度 DH 为 2、6 和 10%)对其理化性质的影响,并确定这些水解产物(0.5、1.0 和 1.5%)形成和稳定油/水乳液的最小浓度。测定了 RPI 及其水解产物(RPH)的理化性质、界面张力(IT)和表面特性。即使在较低的蛋白质浓度(1.0%)下,与较高蛋白质浓度(1.5%)的 RPI 相比,蛋白质水解产物的 IT 也较低。当 RPI 水解时,界面张力从 17.6 mN/m 降低到 9.9 mN/m。此外,酶水解(DH 6%和 10%)在 pH 3-11 范围内使蛋白质溶解度提高了近 20%。通过 IT 和溶解度的结果证实了 RPH 的改进的两亲性质,通过更高的乳液稳定性(由 Turbiscan 和乳液稳定性指数表示)证实了这一点。在较低的蛋白质浓度(1%)下,由 RPH(DH 6%和 10%)稳定的乳液表现出比在较高蛋白质浓度(1.5%)下的 RPI 更好的物理稳定性。在这项工作中,我们验证了形成和稳定油包水(O/W)乳液所需的米蛋白水解产物的最小浓度。

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