Studies on beta-glucanases. Some properties of a bacterial endo-beta-(1 leads to 3)-glucanase system.
A commercial enzyme preparation, originally obtained from a Flavobacterium(Cytophaga), was fractionated by continuous electrophoresis, giving a protein fraction which hydrolysed laminarin, carboxymethylpachyman, barley beta-glucan, lichenin and cellodextrin in random fashion. This enzymic activity was not very stable. Ion-exchange chromatography and molecular-sieve chromatography on Bio-Gel P-60 showed that this activity was due to two specific beta-glucanases, an endo-beta-(1-->3)-glucanase and an endo-beta-(1-->4)-glucanase. The two enzymes occur in both high- and low-molecular-weight forms, the latter endo-beta-(1-->3)-glucanase having a molecular weight of about 16000.
D002852:Chromatography, Ion Exchange; D003956:Dialysis; D004586:Electrophoresis; D005417:Flavobacterium / Q000201:enzymology*; D005959:Glucosidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011134:Polysaccharides; D014462:Ultrafiltration
D011134:Polysaccharides; D005959:Glucosidases