| 光谱学与光谱分析 |
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| Raman Spectroscopy Study Structural Changes in Black Bean Protein Isolate upon Ultrasonic-Treatment |
| YANG Yong1，2, WANG Zhong-jiang2, BI Shuang2, SUI Xiao-nan2, QI Bao-kun2, LI Yang2*, JIANG Lian-zhou2* |
| 1. College of Food Science，Northeast Agricultural University, Harbin 150030，China2. Key Laboratory of Processing Agricultural Products of Heilongjiang Province, College of Food and Bioengineering, Qiqihar University, Qiqihar 161006，China |
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Abstract This article focused on the assessment of the potential of Raman spectroscopy for the determination of structural changes in black-bean protein isolate (BBPI) dispersions with low-frequency (20 kHz) ultrasonication applied at various powers (150, 300 or 450 W) and for different durations (12 or 24 min). It also reported on differential scanning calorimetry analyses. A decrease in TD at low- and medium-power ultrasonication confirmed these ultrasonication treatment disrupted internal hydrophobic interactions of protein molecules and broke up unstable aggregates to smaller soluble protein aggregates, while an increase in TD at high-power was attributed to repolymerization of aggregates. Raman spectroscopy analysis revealed a decrease in the α-helix proportion and an increase in β-sheets after ultrasonic treatment except Sample E (300 W, 24 min). Transformation of aggregation results in a reconstruction in secondary structure of BBPI, especially in β-sheet structure. Ultrasonic-treatment induced a decrease in the normalized intensity of the Raman band near 760 cm-1 which indicated that Tryptophan residues tended to expose and also indicated protein partially unfolding. No significant difference was found in Tyr doublet ratios between unheated and ultrasound-treated BBPI indicated that ultrasound did not change the microenvironment around tyrosyl residues. While the intensity of 1 450 cm-1 band increased with increasing ultrasonic intensity and treatment time, and then decreased with further increase in power and treatment time. In general, the formation of aggregation transferred g-g-t conformation to t-g-t conformation. Though some mechanism of aggregation-repolymerization of BBPI remains to be clearly defined, Raman spectroscopy provide a feasible tool to study the structural changes of BBPI prepared under different ultrasonic conditions, give a new perspective to elucidation of protein structure.
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Received: 2015-10-26
Accepted: 2016-02-05
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Corresponding Authors:
LI Yang, JIANG Lian-zhou
E-mail: liyanghuangyu@163.com;jlzname@163.com
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