An acid exo-β-1,3-d-glucanase was isolated from the commercial digestive enzyme Molsin prepared from Aspergillus saitoi. The enzyme had a molecular weight of 57,000, isoelectric point of pH 4.1, optimum pH of 3.8 and an optimum temperature of 50°C. Major amino acid components of the enzyme were Asx, Ser, Thr and Gly which comprised more than 60% of the molecule, while 11% was carbohydrates. The N-terminal amino acid was determined to be Gly. The enzyme acted on the β-1,3-d-glucan (Pachyman) or laminaritetraose in an exo-type manner and the hydrolysis product was α-d-glucose.
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology