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作 者:吴海涛[1] WU Haitao(School of Science,Heilongjiang Bayi Agricultural University,Daqing 163319,China)
机构地区:[1]黑龙江八一农垦大学理学院,黑龙江大庆163319
出 处:《食品科学》2020年第5期87-92,共6页Food Science
摘 要:探究微射流(0、42.5、89.0、123.5、152.0、175.5 MPa)作用下野生黑豆蛋白结构变化规律,研究表明:微射流处理促进了野生黑豆蛋白质分子间的疏水交互作用,蛋白中的不稳定聚集体逐渐分解成小分子可溶性聚合物,而在超过123.5 MPa时,高强度的剪切作用使可溶性蛋白重新聚合,其乳化性随均质压力增加先增大后减小,乳化稳定性变化不显著(P>0.05)。拉曼光谱分析结果表明:与未处理野生黑豆蛋白相比,微射流均质处理下所有蛋白均发生了α-螺旋结构相对含量增加和β-折叠结构相对含量减少的现象。拉曼光谱在760 cm-1色氨酸归属峰处强度降低,表明均质处理使野生黑豆蛋白发生了部分的解折叠,蛋白表现为"暴露"态。均质处理下酪氨酸归属峰强度显著增加,表明微射流均质处理改变野生黑豆蛋白酪氨酸的微环境。拉曼归属谱带强度随着均质压力的增加而增大,使二硫键的t-g-t型构象转化为g-g-t型构象。The effects of microfluidization applied at different pressures(0, 42.5, 89.0, 123.5, 152.0 and 175.5 MPa) on the structure and solubility of black bean protein isolate(BBPI) from wild black beans were studied. The results showed that microfluidization enhanced the hydrophobic interaction between wild BBPI molecules and caused breakdown of unstable aggregates into soluble proteins. However, high shearing strength at pressure exceeding 123.5 MPa resulted in reaggregation of the soluble proteins. The emulsifying activity of BBPI increased initially and then decreased with increasing pressure, while the emulsion stability did not change significantly(P > 0.05). Raman spectroscopy analysis showed that compared with native BBPI, the contents of α-helical and β-sheet decreased in all simples subjected to microfluidization. Microfluidization resulted in partial unfolding of the proteins and exposure of tryptophan residues on the protein surface as demonstrated by a decrease in the intensity of tryptophan band at 760 cm-1, but it significantly increased the intensity of tyrosine band, indicating that the microenvironment around tyrosine residues was altered. The Raman intensity increased as the homogenization pressure increased, resulting in conformational transformation of disulfide bond from t-g-t to g-g-t.
关 键 词:微射流 野生黑豆蛋白 溶解性 表面疏水性 乳化性 拉曼光谱
分 类 号:TS201.1[轻工技术与工程—食品科学]
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