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

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

Carbohydrate research (2010-12-15)
Alexander M Zakharenko, Mikhail I Kusaykin, Svetlana N Kovalchuk, Stanislav D Anastyuk, Bui Minh Ly, Victoria V Sova, Valeriy A Rasskazov, Tatyana N Zvyagintseva
要旨

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 1380bp contains an open reading frame of 1332bp 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.

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製品内容

Sigma-Aldrich
β-(1→3)-D-グルカナーゼ from Helix pomatia, ≥0.2 U/mg