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Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata
Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata
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Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata
Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata

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Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata
Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata
Journal Article

Catalytic properties and amino acid sequence of endo-1 arrow right 3- beta -D-glucanase from the marine mollusk Tapes literata

2012
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Overview
A specific 1 arrow right 3- beta -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 45dgC. The 1 arrow right 3- beta -D-glucanase catalyzes hydrolysis of beta -1 arrow right 3 bonds in glucans as an endoenzyme with retention of bond configuration, and it has transglycosylating activity. The K sub(m) for hydrolysis of laminaran is 0.25 mg/ml. The enzyme is classified as a glucan endo-(1 arrow right 3)- beta -D-glucosidase (EC 3.2.1.39). The cDNA encoding this 1 arrow right 3- beta -D-glucanase from T. literata was sequenced, and the amino acid sequence of the enzyme was determined. The endo-1 arrow right 3- beta -D-glucanase from T. literata was assigned to the 16th structural family (GHF 16) of O-glycoside hydrolases.
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