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Catalytic Properties and Amino Acid Sequence of Endo-1→3-β-D-glucanase from the Marine Mollusk Tapes literata

A. M. Zakharenko1*, M. I. Kusaykin1, S. N. Kovalchuk1, V. V. Sova1, A. S. Silchenko1, A. A. Belik2, S. D. Anastyuk1, Bui Minh Ly3, V. A. Rasskazov1, and T. N. Zvyagintseva1

1Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, pr. 100 let Vladivostoku 159, 690022 Vladivostok, Russia; E-mail: rarf@yandex.ru

2Far Eastern Federal University, ul. Sukhanova 8, 690950 Vladivostok, Russia

3Nha Trang Institute of Technology Research and Application, Hung Vuong st. 02, Nha Trang, Vietnam

* To whom correspondence should be addressed.

Received February 1, 2012; Revision received May 2, 2012
A specific 1→3-β-D-glucanase with molecular mass 37 kDa was isolated in homogeneous state from crystalline style of the commercial marine mollusk Tapes literata. It exhibits maximal activity within the pH range from 4.5 to 7.5 at 45°C. The 1→3-β-D-glucanase catalyzes hydrolysis of β-1→3 bonds in glucans as an endoenzyme with retention of bond configuration, and it has transglycosylating activity. The Km for hydrolysis of laminaran is 0.25 mg/ml. The enzyme is classified as a glucan endo-(1→3)-β-D-glucosidase (EC The cDNA encoding this 1→3-β-D-glucanase from T. literata was sequenced, and the amino acid sequence of the enzyme was determined. The endo-1→3-β-D-glucanase from T. literata was assigned to the 16th structural family (GHF 16) of O-glycoside hydrolases.
KEY WORDS: 1→3-β-D-glucanase, crystalline style, laminaran, marine mollusk, Tapes literata, transglycosylation

DOI: 10.1134/S0006297912080081