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微波对大豆蛋白氧化聚集体结构及功能特性的影响
引用本文:江连洲, 王一畅, 马依彤, 刘军, 杨宗瑞, 郭增旺. 微波对大豆蛋白氧化聚集体结构及功能特性的影响[J]. 农业工程学报, 2023, 39(9): 261-269. DOI: 10.11975/j.issn.1002-6819.202302061
作者姓名:江连洲  王一畅  马依彤  刘军  杨宗瑞  郭增旺
作者单位:1.东北农业大学食品学院, 哈尔滨 150030;2.山东禹王生态食业有限公司, 德州 253000;3.克东禹王大豆蛋白食品有限公司, 齐齐哈尔 161000
基金项目:山东省重点与研发计划项目(2022CXGC010603);黑龙江省优秀青年科学基金项目(YQ2022C021);黑龙江省百千万工程项目(2021ZX12B02);黑龙江省重点研发计划项目(GA21B001);国家重点研发计划项目(2022YFF1100603);黑龙江省支持重大科技成果转化项目(CG19A002);中国博士后面上项目(2022M721995)
摘    要:为了探究不同时间微波处理对大豆蛋白氧化聚集体的结构和功能性质的影响,由偶氮二异丁脒盐酸盐(2,2'-azobis (2-amidinopropane) dihydrochloride,AAPH)诱导构建大豆蛋白氧化反应体系,采用功率为350 W的微波对其照射不同时间(0、10、20、30、40、50、60、70 s),探究微波处理对氧化聚集大豆蛋白的结构特性和加工特性的影响。结果表明,氧化可诱导形成粒径、分子量更大,结构更致密的蛋白质聚集体,同时对加工特性造成损害。适当时间(<30 s)的微波处理会导致氧化聚集体的分子结构打开、粒径降低和浊度降低,无序结构减少,进而改善了起泡性、乳化性和持水、持油性。长处理时间(>30 s)的微波处理导致已解聚的大豆蛋白分子重新形成更大的分子聚集体,降低功能性质。这表明微波物理场可以通过改变大豆蛋白氧化聚集体的结构和聚集行为调节其功能性质,为大豆蛋白功能性质的改善及微波在大豆蛋白氧化聚集体行为调控的应用方面提供参考。

关 键 词:微波  结构  大豆蛋白  氧化聚集体  功能特性
收稿时间:2023-02-12
修稿时间:2023-04-26

Effects of microwave treatment on the structural and functional properties of oxidized aggregated soybean proteins
JIANG Lianzhou, WANG Yichang, MA Yitong, LIU Jun, YANG Zongrui, GUO Zengwang. Effects of microwave treatment on the structural and functional properties of oxidized aggregated soybean proteins[J]. Transactions of the Chinese Society of Agricultural Engineering (Transactions of the CSAE), 2023, 39(9): 261-269. DOI: 10.11975/j.issn.1002-6819.202302061
Authors:JIANG Lianzhou  WANG Yichang  MA Yitong  LIU Jun  YANG Zongrui  GUO Zengwang
Affiliation:1.College of Food Science, Northeast Agricultural University, Harbin 150030, China;2.Shandong Yuwang Ecogical Food Industry Co., Ltd., Dezhou 253000, China;3.Kedong Yuwang Soybean Protein Food Co., Ltd., Qiqihar 161000, China
Abstract:Soybean protein is widely used as a high-quality plant protein in the food industry, due to its multiple functional properties. However, the high-activity lipoxygenase is easy to catalyze the lipid peroxidation of polyunsaturated fatty acids during the processing of soybean products. A large number of reactive oxygen species and secondary oxidation products can also be produced to further induce protein oxidation. The structure and function of proteins are closely related to the oxidation that is accompanied by the changes in protein solubility, water retention, gel, and emulsification functional properties, thus leading to the processing properties of proteins. Fortunately, microwave processing can be expected to alter the spatial structure of proteins and intermolecular forces. The reaction groups can be exposed to be originally embedded in the protein molecules, resulting in changes in their structure and functional characteristics. Taking the soybean protein oxidized aggregates as the raw materials, this work aims to clarify the effect of microwave treatment time on the functional characteristics and structure, such as solubility, emulsification, and foaming. The protein functional properties were then improved without the use of biochemical reagents, high-pressure, or radiation treatment, thereby expanding the protein applications without the wastes of food resources. An oxidization reaction was constructed with the soy protein and AAPH (2,2''-azobis(2-methylpropionamidine) dihydrochloride). Different irradiation durations (0, 10, 20, 30, 40, 50, 60, and 70 s) of the microwave with a power of 350 W were used to investigate the effect of microwave treatment on the structural characteristics (particle size distribution, turbidity, secondary structure, and microstructure) and processing properties (solubility, water-holding capacity, oil-holding capacity, foaming and foam stability, emulsification and emulsion stability) of oxidized aggregated soy protein. The results showed that the oxidation induced the formation of larger particle size, higher molecular weight, and more compact protein aggregates, which simultaneously damaged the processing properties. Microwave treatment for an appropriate time (<30 s) induced the polarization of protein isolate molecule. There was damage to the non-covalent bond that maintained the protein spatial structure. The protein isolate molecules were partially unfolded to expose the internal hydrophobic residues on the protein surface, thus promoting the formation of the water-air interface. At the same time, the interaction between that extensin molecules formed a more stable interfacial facial mask, thereby improving the foaming, emulsifying, water, and oil-holding properties. Microwave treatment for a long time (>30 s) promoted the further expansion of soy protein isolate molecules, and further exposure inside the hydrophobic and sulfhydryl groups. As such, the larger molecular aggregates were formed between depolymerized protein molecules through noncovalent bonds. There was an increase in the particle size, turbidity, and disordered structure, whereas, a decline in the stability of the interfacial facial mask, thus leading to the decline of functional properties. Consequently, the physical field of microwaves can be expected to modulate the functional properties of soy protein. Specifically, the structural and aggregation behavior can be altered to improve the functional properties of soy protein for the better behavior of soy protein oxidation aggregates using microwaves. The finding can also provide a strong reference for microwave processing in the field of food production.
Keywords:microwave  structureoxidized aggregates  soybean protein  oxidized aggregates  functional properties
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