Cellulases of a marine mollusc, Dolabella sp.
- 1 April 1966
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 99 (1) , 214-221
- https://doi.org/10.1042/bj0990214
Abstract
A crude cellulase extract was prepared from the hepa-topancreas of a marine mollusc, Dolabella sp., and partially purified by ammonium sulphate fractionation. The optimum pH values of the partially purified preparation were 6-5 and 8-0 for Walseth cellulose and CM-cellulose respectively. It was most stable at pH 6-0 and showed moderate thermostability. The partially purified preparation was subjected to starch-zone electrophoresis, and incompletely resolved into several fractions that contained one or more cellulase components of different substrate specificity. Some of these cellulase fractions showed practically no aryl [beta]-glucosidase activity and hydrolysed aryl [beta]-cellobioside with difficulty. From substrates such as higher cello-oligosaccharides, cellodextrin, CM-cellulose, Walseth cellulose and cotton fibre, they produced cellobiose as the major and cellotriose as the minor end products, both of which were resistant to further attack by cellulase. From the slope of the curves of viscosity-reducing power for CM-cellulose, the cellulase components from Dolabella were presumed to be of a "more-random" or a "less-random" type in the mode of action. In the hepatopancreas of this mollusc, [beta]-glucosidases were also present, which hydrolysed cellobiose as well as aryl [beta]-glucosides. The optimum pH values of these enzymes were about 5-5.This publication has 15 references indexed in Scilit:
- Studies on cellulolytic enzymesI. Isolation of a low-molecular-weight cellulase from PolyporusversicolorBiochimica et Biophysica Acta, 1963
- Studies on cellulolytic enzymesII. Multiplicity of the cellulolytic enzymes of Polyporus versicolorBiochimica et Biophysica Acta, 1963
- Partial purification and some properties of a cellulase from Helix pomatiaBiochemical Journal, 1959
- Cellulose-splitting enzymes. VI. Difference in the specificities of cellulase and β-glucosidase from Irpex lacteusArchives of Biochemistry and Biophysics, 1959
- RESOLUTION OF FUNGAL CELLULASE BY ZONE ELECTROPHORESISJournal of Biological Chemistry, 1956
- Purification of Myrothecium verrucaria cellulaseArchives of Biochemistry and Biophysics, 1953
- Notes on sugar determination.1952
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- The carbohydrates of the Jerusalem artichoke and other CompositaeBiochemical Journal, 1950
- Detection of Sugars on Paper ChromatogramsNature, 1950