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Effect of linear charge density of polysaccharides on interactions with α-amylase: Self-Assembling behavior and application in enzyme immobilization

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成果类型:
期刊论文
作者:
Jin, Weiping*;Wang, Zhifeng;Peng, Dengfeng;Shen, Wangyang;Zhu, Zhenzhou;...
通讯作者:
Jin, Weiping
作者机构:
[Cheng, Shuiyuan; Shen, Wangyang; Zhu, Zhenzhou; Jin, Weiping; Huang, Qingrong; Wang, Zhifeng] Wuhan Polytech Univ, Hubei Key Lab Proc & Transformat Agr Prod, Wuhan 430023, Peoples R China.
[Cheng, Shuiyuan; Shen, Wangyang; Zhu, Zhenzhou; Jin, Weiping; Huang, Qingrong; Wang, Zhifeng] Wuhan Polytech Univ, Coll Food Sci & Engn, Wuhan 430023, Peoples R China.
[Huang, Qingrong] Rutgers State Univ, Food Sci, 65 Dudley Rd, New Brunswick, NJ 08901 USA.
[Li, Bin; Peng, Dengfeng] Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China.
通讯机构:
[Jin, Weiping] W
Wuhan Polytech Univ, Hubei Key Lab Proc & Transformat Agr Prod, Wuhan 430023, Peoples R China.
Wuhan Polytech Univ, Coll Food Sci & Engn, Wuhan 430023, Peoples R China.
语种:
英文
关键词:
Complexes coacervation;Enzyme immobilization;Pectin;Self-assembly;α-Amylase;λ-Carrageenan
期刊:
Food Chemistry
ISSN:
0308-8146
年:
2020
卷:
331
页码:
127320
基金类别:
This work is financially supported by the National Natural Science Foundation of China (Grant No. 31801587) and the fund of Hubei Key Laboratory for Processing and Transformation of Agricultural Products (Grant No. 2018HBSQGDKFB03). Finally, thanks to the Shanghai synchrotron radiation source for the equipment provided for SAXS experiments. Thanks to colleagues Yunqi Li and Ce Shi of Changchun Institute of Applied Chemistry for testing.
机构署名:
本校为第一且通讯机构
院系归属:
食品科学与工程学院
摘要:
The co-existence of polysaccharides and enzymes in the food matrix could form complexes that directly influence the catalytic efficacy of enzymes. This work investigated the self-assembly behaviors of α-amylase and charged polysaccharides and fabricated the α-amylase/polysaccharides complex coacervates. The results showed that the linear charge density of polysaccharides had a critical impact on the complex formation, structure, and enzyme protection under acidic conditions. At low pH, α-amylase formed compact and tight coacervates with the ...

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