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Good hydrolysis activity on raffinose family oligosaccharides by a novel alpha-galactosidase from Tremella aurantialba

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成果类型:
期刊论文
作者:
Geng, Xueran;Yang, Dongxue;Zhang, Qiaoyi;Chang, Mingchang;Xu, Lijing;...
通讯作者:
Meng, Junlong;Wang, Hexiang
作者机构:
[Meng, Junlong; Chang, Mingchang; Cheng, Yanfen; Xu, Lijing; Geng, Xueran] Shanxi Agr Univ, Coll Food Sci & Engn, Taigu 030801, Shanxi, Peoples R China.
[Meng, Junlong; Chang, Mingchang; Cheng, Yanfen; Xu, Lijing; Geng, Xueran] Collaborat Innovat Ctr Adv Qual & Efficiency Loes, Taigu 030801, Shanxi, Peoples R China.
[Wang, Hexiang; Yang, Dongxue; Geng, Xueran] China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China.
[Wang, Hexiang; Yang, Dongxue; Geng, Xueran] China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China.
[Zhang, Qiaoyi] Hunan Agr Univ, Orient Sci & Technol Coll, Changsha, Peoples R China.
通讯机构:
[Meng, Junlong] S
[Wang, Hexiang] C
Shanxi Agr Univ, Coll Food Sci & Engn, Taigu 030801, Shanxi, Peoples R China.
China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China.
China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China.
语种:
英文
关键词:
Tremella aurantialba;mushroom;oligosaccharides;alpha-galactosidase
期刊:
International Journal of Biological Macromolecules
ISSN:
0141-8130
年:
2020
卷:
150
页码:
1249-1257
基金类别:
Higher Education Technology Innovation Project in Shanxi [2019L0373]; Doctoral Science Foundation of Shanxi Agricultural University [2017YJ33, 2015YJ04, 2014YJ09]; Reward to Outstanding Doctor Working in Shanxi [SXYBKY201722]; Applied Basic Research Project in Shanxi [201801D221300, 201701D221156]
机构署名:
本校为其他机构
院系归属:
东方科技学院
摘要:
An alpha-galactosidase designated as TAG was purified from the dried fruit bodies of Tremella aurantialba with 182.5-fold purification. The purification procedure involved ion exchange chromatography on Q-sepharose, DEAE-Cellulose, and Mono Q and gel filtration by FPLC on Superdex 75. The purified alpha-galactosidase was a monomeric protein with a molecular mass of 88 kDa. The optimal pH of TAG was 5.0 and more than 60% of the original enzyme activity remained at pH 2.0 and 3.0. Its optimal temperature was 54 degrees C with good thermo-stability, 30.8% of the original activity was retained aft...

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