Substitution of His260 residue alters the thermostability of <i>Pseudoalteromonas carrageenovora</i> arylsulfatase

Yanbing Zhu; Xiaoqian Yin; Han Liu; Hebin Li; Yanhong Chen; Lijun Li; Anfeng Xiao; Hui Ni

doi:10.1007/s13131-019-1356-z

Volume 38 Issue 6

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Yanbing Zhu, Xiaoqian Yin, Han Liu, Hebin Li, Yanhong Chen, Lijun Li, Anfeng Xiao, Hui Ni. Substitution of His260 residue alters the thermostability of Pseudoalteromonas carrageenovora arylsulfatase[J]. Acta Oceanologica Sinica, 2019, 38(6): 75-82. doi: 10.1007/s13131-019-1356-z

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Yanbing Zhu, Xiaoqian Yin, Han Liu, Hebin Li, Yanhong Chen, Lijun Li, Anfeng Xiao, Hui Ni. Substitution of His260 residue alters the thermostability of Pseudoalteromonas carrageenovora arylsulfatase[J]. Acta Oceanologica Sinica, 2019, 38(6): 75-82. doi: 10.1007/s13131-019-1356-z

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Substitution of His260 residue alters the thermostability of Pseudoalteromonas carrageenovora arylsulfatase

doi: 10.1007/s13131-019-1356-z

Yanbing Zhu^{1, 2, 3, 4},
Xiaoqian Yin¹,
Han Liu¹,
Hebin Li⁵,
Yanhong Chen^{1, 2, 3, 4},
Lijun Li^{1, 2, 3, 4},
Anfeng Xiao^{1, 2, 3, 4},
Hui Ni^{1, 2, 3, 4
,
,}

1.
College of Food and Biological Engineering, Jimei University, Xiamen 361021, China
2.
Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China
3.
Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China
4.
Key Laboratory of Systemic Utilization and In-depth Processing of Economic Seaweed, Xiamen Southern Ocean Technology Center of China, Xiamen 361021, China
5.
Department of Pharmacy, Xiamen Medical College, Xiamen 361023, China

Funds: The National Natural Science Foundation of China under contract No. 31401632; the Program for New Century Excellent Talents in Fujian Province University, China under contract No. B15139.

More Information

Corresponding author: E-mail: nihui@jmu.edu.cn
Received Date: 2018-05-23
Accepted Date: 2018-06-22

Available Online: 2020-04-21

Publish Date: 2019-06-01

Abstract

Abstract

This study aimed to improve the thermostability of arylsulfatase from Pseudoalteromonas carrageenovora. A library of P. carrageenovora arylsulfatase mutants was constructed by introducing random mutagenesis using error-prone PCR. After screening, two mutants of H260L and D84A/H260L showed enhanced thermal stability than the wild-type predecessor (WT). Site-directed mutagenesis demonstrated that only amino acid residue at Position 260 plays an important role in the thermostability of P. carrageenovora arylsulfatase. Thermal inactivation analysis showed that the half-life (t_1/2) values at 55°C for H260L, H260I, H260Q, H260F and H260R were 40.6, 48.4, 30.9, 29.1 and 34.5 min, respectively, while that of WT was 9.1 min. Structure modeling demonstrated that the additional hydrogen bonds and/or optimization of surface charge-charge interactions could be responsible for the increased thermostability imparted by H260L, H260I, H260Q, H260F and H260R.
- arylsulfatase,
- Pseudoalteromonas carrageenovora,
- directed evolution,
- error-prone PCR,
- thermostability

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