Enzymatic and molecular characterization of an endo-1,3-β- d-glucanase from the crystalline styles of the mussel Perna viridis

• Published in: Carbohydrate research 2011-02, Vol.346 (2), p.243-252
• Main Authors: Zakharenko, Alexander M., Kusaykin, Mikhail I., Kovalchuk, Svetlana N., Anastyuk, Stanislav D., Ly, Bui Minh, Sova, Victoria V., Rasskazov, Valeriy A., Zvyagintseva, Tatyana N.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; cDNA cloning; DNA, Complementary - genetics; endo-1,3-β- d-Glucanase; Glucan Endo-1,3-beta-D-Glucosidase - chemistry; Glucan Endo-1,3-beta-D-Glucosidase - classification; Glucan Endo-1,3-beta-D-Glucosidase - genetics; Laminaran; Mass-spectrometry; Molecular Sequence Data; Muscles - enzymology; Perna - enzymology; Perna - genetics; Perna viridis; Transglycosylation
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/j.carres.2010.11.008

The retaining endo-1,3-β- d-glucanase (EC 3.2.1.39) was isolated from the crystalline styles of the commercially available Vietnamese edible mussel Perna viridis. It catalyzes hydrolysis of β-1,3-bonds in glucans and enables to catalyze a transglycosylation reaction. Resources of mass-spectrometry for analysis of enzymatic products were studied. cDNA sequence of endo-1,3-β- d-glucanase was determined by RT-PCR in conjunction with the rapid amplification of cDNA ends (RACE) methods. The cDNA of 1380 bp contains an open reading frame of 1332 bp encoding a mature protein of 328 amino acids. On basis of amino acid sequence analysis endo-1,3-β- d-glucanase was classified as a glycoside hydrolase of family 16.