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Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries
被引:9
|作者:
Liu, Lu
[1
,2
]
Guo, Jing
[1
]
Zhou, Xue-Feng
[3
]
Li, Ze
[4
]
Zhou, Hai-Xiang
[1
]
Song, Wei-Qing
[1
]
机构:
[1] Qingdao Municipal Hosp, Dept Clin Lab, Qingdao, Peoples R China
[2] Ocean Univ China, Sch Med & Pharm, Qingdao, Peoples R China
[3] Qingdao Univ, Clin Trial Res Ctr, Affiliated Cent Hosp, Qingdao, Peoples R China
[4] Linyi Vocat Univ Sci & Technol, Coll Adv Agr Sci, Linyi, Shandong, Peoples R China
关键词:
tannin;
tannase;
thermostability;
Aureobasidium melanogenum;
Yarrowia lipolytica;
TANNIN ACYL HYDROLASE;
SOLID-STATE FERMENTATION;
ASPERGILLUS-NIGER;
EXTRACELLULAR TANNASE;
GROWTH-PERFORMANCE;
GALLIC ACID;
STRUCTURAL-CHARACTERIZATION;
BACTERIAL TANNASE;
SOLVENT-TOLERANT;
GREEN TEA;
D O I:
10.3389/fbioe.2021.769816
中图分类号:
Q81 [生物工程学(生物技术)];
Q93 [微生物学];
学科分类号:
071005 ;
0836 ;
090102 ;
100705 ;
摘要:
Being a key industrial enzyme, tannase is extensively applied in various fields. Despite the characterizations of a large number of tannases, there are hardly a few tannases with exceptional thermostability. In this detailed study, a tannase-encoding gene named tanA was identified from Aureobasidium melanogenum T9 and heterologously expressed in Yarrowia lipolytica host of food grade. The purified tannase TanA with a molecular weight of above 63.0 kDa displayed a specific activity of 941.4 U/mg. Moreover, TanA showed optimum activity at 60 degrees C and pH 6.0. Interestingly, TanA exhibited up to 61.3% activity after incubation for 12 h at 55 degrees C, signifying its thermophilic property and distinguished thermostability. Additionally, TanA was a multifunctional tannase with high specific activities to catalyze the degradation of various gallic acid esters. Therefore, this study presents a novel tannase, TanA, with remarkable properties, posing as a potential candidate for food and agricultural processing.
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页数:11
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