Research articles
ScienceAsia 47 (2021):ID 403-409 |doi:
10.2306/scienceasia1513-1874.2021.045
A new neoagarobiose-producing agarase from Vibrio
sp. LA1
Bokun Lina,b,†,*, Yandan Zhengb,c,†, Jingxiao Huanga, Junkang Shanga, Yuli Yua,b, Zhong Hub,*
ABSTRACT: An agarolytic bacterium was isolated from the sea coast of Shantou in China and identified as Vibrio sp.
LA1. The agarase gene agaA was cloned from Vibrio sp. LA1 by using degenerate oligonucleotide-primed PCR and
genome walking technique. Gene agaA consists of a 2913 bp open reading frame encoding 970 amino acids; and the
predicted molecular mass and isoelectric point were 108 kDa and 4.46, respectively. Based on the amino acid sequence
similarity, the encoded protein (AgaA) of gene agaA should be an agarase of glycoside hydrolase family GH50 with
a catalytic domain of glycoside hydrolase family GH42. Soluble expression of AgaA in Escherichia coli was obtained
and investigated. The optimal temperature and pH for the activity of the purified recombinant agarase were 35 ?C and
pH 6, respectively. The reducing reagent ?-mercaptoethanol could increase the activity of agarase AgaA by more than
80%. AgaA showed exo-lytic activity on agarose degradation. It decomposed agarose to yield neoagarobiose as the
sole product, which was different from the agarase Aga41A from Vibrio sp. CN41 that showed 95% identities of amino
acid sequence to agarase AgaA. With single end product, purification procedure is easier than that with multi-products.
Therefore, agarase AgaA could be a useful tool for producing the bioactive neoagarobiose.
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| a |
Dongguan Key Laboratory of Environmental Medicine, School of Public Health, Guangdong Medical
University, Dongguan 523808 China |
| b |
Department of Biology, Shantou University, Shantou 515063 China |
| c |
Training & Information Center, Jieyang Polytechnic, Jieyang 522000 China |
* Corresponding author, E-mail: bklin@gdmu.edu.cn, hzh@stu.edu.cn
Received 23 Sep 2020, Accepted 15 Mar 2021
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