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Journal of Biochemistry Advance Access published online on August 22, 2006
Journal of Biochemistry, doi:10.1093/jb/mvj180
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© 2006 The Japanese Biochemical Society.
Received June 11, 2006
Accepted August 6, 2006

Regular Paper

A Novel Enzyme, {lambda}-Carrageenase, Isolated from a Deep-Sea Bacterium

Yukari Ohta 1 * and Yuji Hatada 1

1 Japan Agency for Marine-Earth Science and Technology (JAMSTEC), 2-15 Natsushima, Yokosuka 237-0061, Japan

* To whom correspondence should be addressed.
Yukari Ohta, E-mail: ohtay{at}jamstec.go.jp


  Abstract

A {lambda}-carrageenan-degrading Pseudoalteromonas bacterium, strain CL19, was isolated from a deep-sea sediment sample. A {lambda}-carrageenase from the isolate was purified to homogeneity from cultures containing {lambda}-carrageenan as a carbon source. This is the first report of the isolation of {lambda}-carrageenase together with the gene sequence for the enzyme. The molecular mass of the purified enzyme was approximately 100 kDa on both SDS-PAGE and gel-filtration chromatography, suggesting that the enzyme is a monomer. The optimal pH and temperature for activity were about 7 and 35°C, respectively. The enzyme had specific activity of 253 U/mg protein. The enzyme required monovalent salts for the activity. Carbohydrates, such as sorbitol, sucrose, trehalose, improved the enzyme stability. The pattern of {lambda}-carrageenan hydrolysis showed that the enzyme is an endo-type {lambda}-carrageenase, and the final main product was a tetrasaccharide of the {lambda}-carrageenan ideal structure with galactose 2,6-disulfate at the reducing end, indicating the enzyme cleaves the {beta}-1,4 linkages of its backbone structure. Furthermore, the gene (cglA) encoding the enzyme was sequenced. It encoded a mature protein of 103 kDa (917 amino acids). Remarkably, the deduced amino acid sequence showed no similarity to any reported proteins.

Keywords: cloning; endo-{beta}-1,4-carrageenose 2,6,2'-trisulfate-hydrolase; {lambda}-carrageenan; {lambda}-carrageenase; sequence.
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