NDLI: Hyper-production and Characterization of the ι-Carrageenase Useful for ι-Carrageenan Oligosaccharide Production from a Deep-sea Bacterium, Microbulbifer thermotolerans JAMB-A94T, and Insight into the Unusual Catalytic Mechanism

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Hyper-production and Characterization of the ι-Carrageenase Useful for ι-Carrageenan Oligosaccharide Production from a Deep-sea Bacterium, Microbulbifer thermotolerans JAMB-A94T, and Insight into the Unusual Catalytic Mechanism

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Marine Biotechnology : Volume 13, Issue 2, April 2011

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Hyper-production and Characterization of the ι-Carrageenase Useful for ι-Carrageenan Oligosaccharide Production from a Deep-sea Bacterium, Microbulbifer thermotolerans JAMB-A94T, and Insight into the Unusual Catalytic Mechanism

Content Provider	Springer Nature Link
Author	Hatada, Yuji Mizu, Masahiro Li, Zhijun Ohta, Yukari
Copyright Year	2010
Abstract	A gene of unknown function from the genome of the agar-degrading deep-sea bacterium Microbulbifer thermotolerans JAMB-A94T was functionally identified as a ι-carrageenase gene. This gene, designated as cgiA, is located together with two β-agarase genes, agaA and agaO in a cluster. The cgiA gene product is 569 amino acids and shares 29% identity over 185 amino acids with the ι-carrageenase from Zobellia galactanivorans Dsij DSM 12802. Recombinant, cgiA-encoded ι-carrageenase (55 kDa) was hyper-produced in Bacillus subtilis. The recombinant enzyme shows maximal activity at 50°C, the highest reported optimal temperature for a carrageenase. It cleaved β-1,4 linkages in ι-carrageenan to produce a high ratio of ι-carrageenan tetramer, more than 75% of the total product, and did not cleave the β-1,4 linkages in κ- or λ-carrageenan. Therefore, this enzyme may be useful for industrial production of ι-carrageenan oligosaccharides, which have demonstrated antiviral potential against diverse viruses. Furthermore, we performed site-directed mutagenesis on the gene to identify the catalytic amino acid residues. We demonstrated that a conserved Glu351 was essential for catalysis; however, this enzyme lacked a catalytic Asp residue, which is generally critical for the catalytic activity of most glycoside hydrolases.
Starting Page	411
Ending Page	422
Page Count	12
File Format	PDF
ISSN	14362228
Journal	Marine Biotechnology
Volume Number	13
Issue Number	3
e-ISSN	14362236
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-08-05
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Deep-sea ι-Carrageenan 4-β-D-glycanohydrolase ι-Carrageenase Microbulbifer thermotolerans Sequence Freshwater & Marine Ecology Microbiology Engineering Zoology
Content Type	Text
Resource Type	Article
Subject	Aquatic Science Biotechnology

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