Literature DB >> 16346337

Comparison of beta-Glucosidase Activities in Different Streptomyces Strains.

N Moldoveanu1, D Kluepfel.   

Abstract

Cellobiase (beta-glucosidase) production was compared for two streptomycetes: Streptomyces flavogriseus, a known producer of cellulase complex, and Streptomyces sp. strain CB-12, a strain isolated for its rapid growth on cellobiose. The optimal conditions for enzyme activity were established in relation to pH, temperature, enzyme stability, and substrate affinity. The production of beta-glucosidase by the two strains depended on the carbon substrate in the medium. Cellobiose was found to repress the biosynthesis of the enzyme in S. flavogriseus and to stimulate its production in strain CB-12. The biosynthesis of the enzyme correlated well with the accumulation of glucose in the culture filtrates. The combined action of the beta-glucosidases produced by the two Streptomyces strains might allow a better utilization of the reaction products which arise during the biodegradation of cellulose.

Entities:  

Year:  1983        PMID: 16346337      PMCID: PMC239260          DOI: 10.1128/aem.46.1.17-21.1983

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  14 in total

1.  Measurement of saccharifying cellulase.

Authors:  M Mandels; R Andreotti; C Roche
Journal:  Biotechnol Bioeng Symp       Date:  1976

2.  Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.

Authors:  W Stoppok; P Rapp; F Wagner
Journal:  Appl Environ Microbiol       Date:  1982-07       Impact factor: 4.792

3.  Beta-glucosidase of Trichoderma: its biosynthesis and role in saccharification of cellulose.

Authors:  D Sternberg
Journal:  Appl Environ Microbiol       Date:  1976-05       Impact factor: 4.792

4.  The mechanism of enzymatic cellulose degradation. Isolation and some properties of a beta-glucosidase from Trichoderma viride.

Authors:  L E Berghem; L G Pettersson
Journal:  Eur J Biochem       Date:  1974-07-15

5.  Partial purification and characterization of a new intracellular beta-glucosidase of Trichoderma reesei.

Authors:  M Inglin; B A Feinberg; J R Loewenberg
Journal:  Biochem J       Date:  1980-02-01       Impact factor: 3.857

6.  Repression of endo-1,4-beta-glucanase formation in Penicillium janthinellum and product inhibition of its 1,4-beta-glucanases and cellobiases.

Authors:  P Rapp; U Knobloch; F Wagner
Journal:  J Bacteriol       Date:  1982-02       Impact factor: 3.490

Review 7.  Beta-Glucosidase: its role in cellulase synthesis and hydrolysis of cellulose.

Authors:  J G Shewale
Journal:  Int J Biochem       Date:  1982

8.  Stability of the cellulase of Trichoderma reesei under use conditions.

Authors:  E T Reese; M Mandels
Journal:  Biotechnol Bioeng       Date:  1980-02       Impact factor: 4.530

9.  Derepressed synthesis of cellulase by Cellulomonas.

Authors:  B J Stewart; J M Leatherwood
Journal:  J Bacteriol       Date:  1976-11       Impact factor: 3.490

10.  beta-Glucosidase: microbial production and effect on enzymatic hydrolysis of cellulose.

Authors:  D Sternberg; P Vijayakumar; E T Reese
Journal:  Can J Microbiol       Date:  1977-02       Impact factor: 2.419

View more
  3 in total

1.  Differential Expression of Xylanases and Endoglucanases in the Hybrid Derived from Intergeneric Protoplast Fusion between a Cellulomonas sp. and Bacillus subtilis.

Authors:  D V Gokhale; D N Deobagkar
Journal:  Appl Environ Microbiol       Date:  1989-10       Impact factor: 4.792

2.  Purification and properties of a stable beta-glucosidase from an extremely thermophilic anaerobic bacterium.

Authors:  M L Patchett; R M Daniel; H W Morgan
Journal:  Biochem J       Date:  1987-05-01       Impact factor: 3.857

3.  Purification and properties of a xylanase from Streptomyces lividans.

Authors:  R Morosoli; J L Bertrand; F Mondou; F Shareck; D Kluepfel
Journal:  Biochem J       Date:  1986-11-01       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.