Literature DB >> 5965338

Cellulases of a marine mollusc, Dolabella sp.

G Okada, T Nisizawa, K Nisizawa.   

Abstract

1. A crude cellulase extract was prepared from the hepatopancreas of a marine mollusc, Dolabella sp., and partially purified by ammonium sulphate fractionation. 2. 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 pH6.0 and showed moderate thermostability. 3. 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. 4. 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. 5. 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. 6. 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.

Entities:  

Mesh:

Substances:

Year:  1966        PMID: 5965338      PMCID: PMC1264977          DOI: 10.1042/bj0990214

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  14 in total

1.  Distinctive properties of beta-glucosidases and related enzymes derived from a commercial Aspergillus niger cellulase.

Authors:  K W KING; R M SMIBERT
Journal:  Appl Microbiol       Date:  1963-07

2.  Studies on cellulolytic enzymes. II. Multiplicity of the cellulolytic enzymes of Polyporus versicolor.

Authors:  G PETTERSSON; J PORATH
Journal:  Biochim Biophys Acta       Date:  1963-01-08

3.  Studies on celluloytic enzymes. I. Isolation of a low-molecular-weight cellulase from Polyporus versicolor.

Authors:  G PETTERSSON; E B COWLING; J PORATH
Journal:  Biochim Biophys Acta       Date:  1963-01-08

4.  Partial purification and some properties of a cellulase from Helix pomatia.

Authors:  F L MYERS; D H NORTHCOTE
Journal:  Biochem J       Date:  1959-04       Impact factor: 3.857

5.  Cellulose-splitting enzymes. VI. Difference in the specificites of cellulase and beta-glucosidase from Irpex lacteus.

Authors:  K NISIZAWA; Y HASHIMOTO
Journal:  Arch Biochem Biophys       Date:  1959-03       Impact factor: 4.013

6.  Resolution of fungal cellulase by zone electrophoresis.

Authors:  G L MILLER; R BLUM
Journal:  J Biol Chem       Date:  1956-01       Impact factor: 5.157

7.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

8.  The carbohydrates of the Jerusalem artichoke and other Compositae.

Authors:  J S D BACON; J EDELMAN
Journal:  Biochem J       Date:  1951-01       Impact factor: 3.857

9.  Detection of sugars on paper chromatograms.

Authors:  W E TREVELYAN; D P PROCTER; J S HARRISON
Journal:  Nature       Date:  1950-09-09       Impact factor: 49.962

10.  The biological degradation of soluble cellulose derivatives and its relationship to the mechanism of cellulose hydrolysis.

Authors:  E T REESE; R G H SIU; H S LEVINSON
Journal:  J Bacteriol       Date:  1950-04       Impact factor: 3.490

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.