Catalytic properties of endo-1,3-β-D-glucanase from the Vietnamese edible mussel Perna viridis

Abstract

A beta-1,3-glucanase with a molecular mass of 33 kDa was isolated in the homogeneous state from a crystalline stalk of the commercially available Vietnamese edible mussel Perna viridis. It hydrolyzes beta-1,3-bonds in glucans and is capable of catalyzing the transglycosylation reaction. The beta-1,3-glucanase has a K(m) value of 0.3 mg/ml for the hydrolysis of laminaran and shows a maximum activity in the pH range from 4 to 6.5 and at 45 degrees C. Its half-inactivation time is 180 min at 45 degrees C and 20 min at 50 degrees C. The enzyme was ascribed to glucan-endo-(1-3)-beta-D-glucosidases (EC 3.2.1.39). The enzyme could be used in the structure determination of beta-1,3-glucans and enzymatic synthesis of new carbohydrate-containing compounds.

Dietary substitution of microalgae with the Saccharomyces cerevisiae mutant, Δmnn9, for feeding Pacific oyster (Crassostrea gigas) juveniles

“…Since the cell wall of this mutant is mainly composed of β-1,3-glucan, β-1,3-glucanases are probably the major digestive enzymes participating in the cell-wall digestion. The catalytic property of β-1,3-glucanases has been previously described in bivalves (Kovalchuk et al, 2006;Zakharenko et al, 2009). In the present study, the expression of Cg-βGBP was higher in oysters fed on Δmnn9 than those fed on microalgae or wild-type yeast.…”

Characterization and cytotoxic activity of sulfated derivatives of polysaccharides from Agaricus brasiliensis

“…FR was characterized as a glucan, with a majority of β-(1→6) linkages, and a minor amount of (1→3)-β-linkages. The β-(1→3)-linked H-1 of the side chain appeared as one resolved doublet centered at 4.95 ppm, whose coupling constant value ( J = 8.28 Hz) designates the β-configuration [46, 47]. Although the signal around 86 ppm ascribed to C-3 of (1→3)-β-linkage was not detected in the FR spectrum, as reported by Ohno et al [48], the remaining signals indicate the presence of a (1→3)-β-glucan component.…”

Sự phân bố và đặc tính xúc tác của β-1,3-glucanase ở động vật biển không xương sống Việt Nam

“…Năm 2010, chúng tôi đã nghiên cứu sàng lọc hoạt tính O-glycosyl hydrolase của hơn 80 mẫu động vật không xương sống biển Việt Nam [3]. Một số mẫu trong chúng đã được nghiên cứu tách chiết, tinh sạch và khảo sát đặc tính của enzym thủy phân các polysaccharide như fucoidan, laminaran, polymanuronic acid … Trong đó, β-1,3-glucanase đã được tinh sạch từ sợi thủy tinh thể của Vẹm xanh Perna viridis [1]; enzym thủy phân polymanuronic acid từ gan tụy Ốc bàn tay quéo Lambis sp. cũng đã được tinh sạch [3].…”