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β-1, 3 -Glucanase Produced by Alkalophilic Bacteria Bacillus No. K-12-5

1973; Oxford University Press; Volume: 37; Issue: 6 Linguagem: Inglês

10.1080/00021369.1973.10860853

1881-1280

Koki Horikoshi, Yoko Atsukawa,

Enzyme Production and Characterization

Bacillus No. K–12–5 isolated from soil produced a β-1,3-glucanase in alkaline media. The characteristic point of this bacteria was especially good growth in alkaline media, and no growth was observed in neutral media such as nutrient broth. The β-1,3-glucanase of Bacillus No. K–12–5 was purified by DEAE-cellulose, Sephadex G–100 and hydroxyl apatite columns. The enzyme was most active at pH 5.5 ~ 8.0 which was much broader and higher than those of Bacillus criculans enzyme. The sedimentation constant was about 3.6 and molecular weight was about 40,000. The isoelectric point was about pH 3.5 and the enzyme was most stable at pH 7. Calcium ion was not effective to stabilize the enzyme. The enzyme did not hydrolyse laminaritriose. Laminaritetraose was hydrolysed, and glucose and laminaritriose were detected in the hydrolysate. The enzyme split laminaran at random and yielded glucose, laminaribiose, laminaritriose and higher oligosaccharides. If the enzyme is a single entity, it is a type of endo-β-1,3-glucanase. However, activity of hydrolysis of fungal cell walls was lower than that of B. circulans enzyme.