Gelation potential of oat protein isolate: Influence of extraction method, gelling conditions, and enzymatic modification

IF 9.8 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Chemistry Pub Date : 2025-03-21 DOI:10.1016/j.foodchem.2025.143968

Miikka Laitinen, Tiina Kokkonen, Xin Huang, Kirsi Jouppila, Ndegwa H. Maina, Noora Mäkelä-Salmi

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Abstract

The poor technological functionality of oat protein presents a challenge in food applications. This study investigated the effect of extraction method, gelling conditions (pH and NaCl concentration), and enzymatic modification on heat-induced gelation of oat protein isolate (OPI). Fairly strong gels (G′ = 5000 Pa, tan δ = 0.26) were formed from OPI, but gelation was highly sensitive to pH and NaCl concentration. Extraction at pH ∼10 negatively affected the gelation properties compared to extraction at pH 8. Partial hydrolysis with alcalase, bromelain, or papain increased the solubility of OPI but was detrimental to gelation, leading to liquid expulsion from the gel. After enzymatic deamidation with protein glutaminase, up to 87 % solubility of OPI at pH 7 was achieved, and it formed soft, elastic, and slightly translucent gels (G′ = 1100 Pa, tan δ = 0.21). The extraction process and modifications of oat proteins have a great impact on their techno-functionality and need optimization for food applications.

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燕麦分离蛋白的凝胶势：提取方法、凝胶条件和酶修饰的影响

燕麦蛋白的技术功能差，给食品应用带来了挑战。研究了提取方法、胶凝条件（pH和NaCl浓度）和酶修饰对燕麦分离蛋白（OPI）热致胶凝的影响。OPI形成了较强的凝胶（G′ = 5000 Pa, tan δ = 0.26），但凝胶对pH和NaCl浓度高度敏感。与pH 8的萃取相比，pH ~10的萃取对胶凝性能有负面影响。alcalase、菠萝蛋白酶或木瓜蛋白酶的部分水解增加了OPI的溶解度，但不利于凝胶化，导致液体从凝胶中排出。经蛋白谷氨酰胺酶脱酰胺后，OPI在pH 7下的溶解度可达87 %，形成柔软、有弹性、微半透明的凝胶（G′ = 1100 Pa, tan δ = 0.21）。燕麦蛋白的提取工艺和修饰对其技术功能有很大影响，需要对其进行优化以适应食品应用。

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来源期刊

Food Chemistry 工程技术-食品科技

CiteScore

16.30

自引率

10.20%

发文量

3130

审稿时长

122 days

期刊介绍： Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.