Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Purification and Characterization of an Exo β-1, 3-Glucanase from a Fungi Imperfecti
Susumu NAGASAKIKazuo SAITOShinpei YAMAMOTO
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1977 Volume 41 Issue 3 Pages 493-502

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Abstract

An exo β-1, 3-glucanase has been purified from the culture fluid of a Fungi Imperfecti which had been used for the production of a yeast cell lytic enzyme, Method for the purification of the enzyme involved ammonium sulfate fractionation, column chromatography on DEAE-Sephadex A-50, BioGel P-150 and SE-Sephadex C-50, and affinity chromatography using powdered pachyman prepared from a Chinese medicine “Bukuryo, ” Poria cocos Wolf.
The molecular weight of the enzyme was determined to be 43, 000 by the molecular sieve method using BioGel P-60. The enzyme removes single glucosyl residues successively from the non reducing terminus of β-1, 3-glucan with inversion of configuration. The enzyme has comparatively narrow pH optima with an optimum pH of 6.0 and is most active at 50°C. The Km values of the enzyme for laminarin, laminarihexaose, laminaripentaose, and laminaritetraose are 0.066, 0.83, 2.30, and 18.60 (×10-3M), respectively. Some other properties of the enzyme are also described.

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