Cloning, expression and characterization of a new ι-carrageenase from marine bacterium, Cellulophaga sp.

Abstract:

PURPOSE OF WORK:The purpose of this study is to report a ι-carrageenase which degrades ι-carrageenan yielding neo-ι-carratetraose as the main product in the absence of NaCl. The gene for a new ι-carrageenase, CgiB_Ce, from Cellulophaga sp. QY3 was cloned and sequenced. It comprised an ORF of 1,386 bp encoding for a protein of 461 amino acid residues. From its sequence analysis, CgiB_Ce is a new member of GH family 82 and shared the highest identity of 32% in amino acids with ι-carrageenase CgiA2 from Zobellia galactanovorans indicating that it is a hitherto uncharacterized protein. The recombinant CgiB_Ce had maximum specific activity (1,870 U/mg) at 45 °C and pH 6.5. It was stable between pH 6.0-9.6 and below 40 °C. Although its activity was enhanced by NaCl, the enzyme was active in the absence of NaCl. CgiB_Ce is an endo-type ι-carrageenase that hydrolyzes β-1,4-linkages of ι-carrageenan, yielding neo-ι-carratetraose as the main product (more than 80% of the total product).

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Ma S,Tan YL,Yu WG,Han F

doi

10.1007/s10529-013-1244-0

subject

Has Abstract

pub_date

2013-10-01 00:00:00

pages

1617-22

issue

10

eissn

0141-5492

issn

1573-6776

journal_volume

35

pub_type

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