Raman Spectroscopy Study Structural Changes in Black Bean Protein Isolate upon Ultrasonic-Treatment.

超声 拉曼光谱 差示扫描量热法 蛋白质聚集 超声波传感器 化学 分析化学(期刊) 生物物理学 光谱学 色谱法 生物化学 光学 生物 量子力学 热力学 物理 声学
作者
Yong Yang,Zhongjiang Wang,Shuang Bi,Xiaonan Sui,Baokun Qi,Li Yang,Lianzhou Jiang
出处
期刊:PubMed 卷期号:36 (7): 2318-24 被引量:4
链接
标识
摘要

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.

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
大幅提高文件上传限制,最高150M (2024-4-1)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
KeCoKeLe发布了新的文献求助10
刚刚
MM11111完成签到,获得积分10
1秒前
1秒前
小二郎应助楠楠2001采纳,获得10
1秒前
南宫代萱发布了新的文献求助10
1秒前
2秒前
美好乐松应助申木采纳,获得10
2秒前
3秒前
彭于晏应助Seaton采纳,获得10
3秒前
科研通AI2S应助现实的醉波采纳,获得10
4秒前
zzr元亨利贞完成签到,获得积分10
4秒前
5秒前
6秒前
8秒前
万能小铃铛完成签到,获得积分20
8秒前
8秒前
ZZH完成签到,获得积分10
9秒前
xh完成签到,获得积分10
9秒前
无名之辈发布了新的文献求助10
9秒前
搜集达人应助starying采纳,获得10
10秒前
10秒前
cc123完成签到,获得积分10
10秒前
脑洞疼应助小赵采纳,获得10
10秒前
11秒前
果酱君发布了新的文献求助20
11秒前
CipherSage应助呀呀呀采纳,获得10
11秒前
11秒前
fanfan完成签到,获得积分10
12秒前
Liao发布了新的文献求助10
12秒前
12秒前
shi发布了新的文献求助10
13秒前
14秒前
高大豌豆完成签到 ,获得积分10
15秒前
15秒前
11发布了新的文献求助10
15秒前
15秒前
16秒前
顾矜应助chenyi采纳,获得10
16秒前
17秒前
orixero应助云_123采纳,获得10
18秒前
高分求助中
Evolution 2024
Experimental investigation of the mechanics of explosive welding by means of a liquid analogue 1060
Die Elektra-Partitur von Richard Strauss : ein Lehrbuch für die Technik der dramatischen Komposition 1000
CLSI EP47 Evaluation of Reagent Carryover Effects on Test Results, 1st Edition 600
大平正芳: 「戦後保守」とは何か 550
Sustainability in ’Tides Chemistry 500
Cathodoluminescence and its Application to Geoscience 500
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 基因 遗传学 催化作用 物理化学 免疫学 量子力学 细胞生物学
热门帖子
关注 科研通微信公众号,转发送积分 3008117
求助须知:如何正确求助?哪些是违规求助? 2667352
关于积分的说明 7235471
捐赠科研通 2304596
什么是DOI,文献DOI怎么找? 1222025
科研通“疑难数据库(出版商)”最低求助积分说明 595385
版权声明 593410