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Enhancing the Usability of Pea Protein Isolate in Food Applications through Modifying Its Structural and Sensory Properties via Deamidation by Glutaminase.
Journal of Agricultural and Food Chemistry ( IF 5.7 ) Pub Date : 2020-01-30 , DOI: 10.1021/acs.jafc.9b06046
Luyi Fang 1 , Huan Xiang 1 , Dongxiao Sun-Waterhouse 1 , Chun Cui 1, 2 , Junjie Lin 1
Affiliation  

This study aimed to demonstrate the feasibility of improving the properties of pea protein isolate (PPI) related to food applications via deamidation with glutaminase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FT-IR) profiling revealed that the current glutaminase treatment did not change the basic protein subunit composition. However, it allowed a certain extent of protein unfolding and conformational reorganization to generate more flexible and extended proteins with reduced average particle size and more hydrophobic groups exposed. The underlying mechanisms might include the reduction of β-sheets and antiparallel β-sheets and the increase of the β-turn structure. Moreover, the treatment time was of importance. A 12 h treatment was generally better than a 24 h treatment, and PPI treated with glutaminase at 50 °C for 12 h to a degree of deamidation of 56.1% exhibited significantly improved solubility, homogeneity, dispersibility, and suspendability with reduced beany flavor, grittiness, and lumpiness (compared to those of the untreated PPI). Thus, the glutaminase treatment offers a promising approach for enhancing the usability and applicability of pea proteins.

中文翻译:


通过谷氨酰胺酶脱酰胺作用改变豌豆分离蛋白的结构和感官特性,增强豌豆分离蛋白在食品应用中的可用性。



本研究旨在证明通过谷氨酰胺酶脱酰胺来改善与食品应用相关的豌豆分离蛋白 (PPI) 特性的可行性。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)和傅里叶变换红外(FT-IR)分析表明,当前的谷氨酰胺酶处理没有改变基本蛋白质亚基组成。然而,它允许一定程度的蛋白质解折叠和构象重组,以产生更灵活和延伸的蛋白质,具有减小的平均粒径和更多的疏水基团暴露。潜在机制可能包括β-折叠和反平行β-折叠的减少以及β-转角结构的增加。此外,治疗时间也很重要。 12小时处理通常优于24小时处理,并且用谷氨酰胺酶在50℃处理12小时至脱酰胺度为56.1%的PPI表现出显着改善的溶解度、均质性、分散性和悬浮性,同时减少豆味、砂砾感和块度(与未经处理的 PPI 相比)。因此,谷氨酰胺酶处理为增强豌豆蛋白的可用性和适用性提供了一种有前途的方法。
更新日期:2020-01-31
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