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食品与发酵工业  2019, Vol. 45 Issue (1): 100-108    DOI: 10.13995/j.cnki.11-1802/ts.016995
  研究报告 本期目录 | 过刊浏览 | 高级检索 |
pH偏移结合温和热处理对蚕豆分离蛋白结构和功能的影响
周向军,董瑞红,高义霞
(天水师范学院 生物工程与技术学院,甘肃 天水,741001)
Effects of pH-shifting combined with mild heating processes on structural and functional properties of broad bean protein isolates
ZHOU Xiangjun, DONG Ruihong, GAO Yixia
(College of Bioengineering and Technology, Tianshui Normal University, Tianshui 741001,China)
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摘要 研究pH偏移结合温和热处理对蚕豆分离蛋白(broad bean protein isolate, BBPI)结构和功能的影响。BBPI在pH1.5结合25、37和55 ℃条件下,分别处理0、1.5、3.5和5.5 h后,逐渐恢复至中性,分析其溶解性、乳化性、巯基/总巯基含量、紫外、荧光光谱、表面疏水性、二级结构含量和微结构变化。结果表明:随时间延长,BBPI溶解性和乳化性均先降低后增加,37和55 ℃处理组巯基含量先增加后降低,25 ℃处理组则变化不大。随时间延长,37 ℃处理组总巯基含量先增加后迅速下降,25和55 ℃先平稳后降低。紫外和荧光光谱表明,随时间延长,25 ℃处理的大部分色氨酸残基包裹在分子内部疏水微环境,37 ℃处理组的色氨酸残基部分解折叠。25和37 ℃处理时,BBPI的表面疏水性先增加后降低,55 ℃处理则先增加后出现波动。随温度增加,BBPI的α-螺旋和β-折叠逐渐转化为β-转角和无规则卷曲,形成粒径约80~130 nm的球状体且存在团聚。pH偏移结合温和热处理在一定程度上可改变蚕豆分离蛋白的结构和功能。
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周向军
董瑞红
高义霞
关键词:  蚕豆分离蛋白  pH偏移  热处理  结构    
Abstract: Effects of pH-shifting combined with mild heating process on structural and functional properties of broad bean protein isolateS(BBPI) were investigated. The BBPI underwent heat treatment (25 ℃, 37 ℃ and 55 ℃) at pH=1.5 for 0, 1.5 h, 3.5 h, and 5.5 h, respectively, followed by refolding at neutral pH. Changes in its solubility, emulsification, sulfhydryl/total sulfhydryl content, UV and fluorescence spectrum, surface hydrophobicity, secondary structure content, and microstructure were explored. The results showed that both solubility and emulsification decreased first and then increased with time. The sulfhydryl content increased first and then decreased at 37 ℃ and 55 ℃, respectively, and it remained almost unchanged at 25 ℃. At 37 ℃, total sulfhydryl content increased first and decreased rapidly. It remained almost stable at the beginning and reduced at 25 ℃ and 55 ℃, respectively. UV and fluorescence spectroscopy revealed that most of the tryptophan(Trp) residues were wrapped and located mainly in the hydrophobic area in the inner core of BBPI at 25 ℃. However, the Trp residues were found unfolded at 37 ℃. Surface hydrophobicity of BBPI increased first and then decreased at 25 ℃ and 37 ℃, respectively, but it increased and then fluctuated at 55 ℃. As temperature increasing, the α-helical and β-sheet of BBPI gradually transformed into β-turn and random coil, and the particles were spherical agglomerates with average diameter around 80-130 nm. Therefore, it was concluded that structural and functional properties of BBPI could be changed via pH-shifting combined with mild heating process to some extent.
Key words:  broad bean protein isolates    pH-shifting    heating processes    structure
收稿日期:  2018-02-01                出版日期:  2019-01-15      发布日期:  2019-02-01      期的出版日期:  2019-01-15
基金资助: 天水市科技支撑项目(苹果疏除果实中苹果多酚的生产及降血压成分的分离、鉴定)
作者简介:  硕士,副教授。
引用本文:    
周向军,董瑞红,高义霞. pH偏移结合温和热处理对蚕豆分离蛋白结构和功能的影响[J]. 食品与发酵工业, 2019, 45(1): 100-108.
ZHOU Xiangjun,DONG Ruihong,GAO Yixia. Effects of pH-shifting combined with mild heating processes on structural and functional properties of broad bean protein isolates[J]. Food and Fermentation Industries, 2019, 45(1): 100-108.
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