Abstract
A strain of bakers' yeast was isolated which could utilize cellobiose and other β-D-glucosides quantitatively as carbon and energy sources for growth. Cellobiose-grown cells contained a largely cryptic enzyme active against the chromogenic substrate p-nitrophenyl-β-D-glucoside. The patent (intact cell) activity of such cells was inhibited by azide and, competitively, by cellobiose; neither agent inhibited the β-glucosidase activity of lysed cells or of extracts. The enzyme induced by growth in cellobiose medium had no affinity for cellobiose as either substrate or inhibitor; its substrate specificity classifies it as an aryl-β-glucosidase. It was concluded that growth in cellobiose also induced the formation of a stereospecific and energy-dependent system whose function determined the rate at which intact cells could hydrolyze substrates of the intracellular β-glucosidase.
Full Text
The Full Text of this article is available as a PDF (672.7 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- AYERS W. A. Phosphorolysis and synthesis of cellobiose by cell extracts from Ruminococcus flavefaciens. J Biol Chem. 1959 Nov;234:2819–2822. [PubMed] [Google Scholar]
- AYERS W. A. Phosphorylation of cellobiose and glucose by Ruminococcus flavefaciens. J Bacteriol. 1958 Nov;76(5):515–517. doi: 10.1128/jb.76.5.515-517.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BARNETT J. A., INGRAM M., SWAIN T. The use of beta-glucosides in classifying yeasts. J Gen Microbiol. 1956 Dec;15(3):529–555. doi: 10.1099/00221287-15-3-529. [DOI] [PubMed] [Google Scholar]
- DUERKSEN J. D., HALVORSON H. Purification and properties of an inducible beta-glucosidase of yeast. J Biol Chem. 1958 Nov;233(5):1113–1120. [PubMed] [Google Scholar]
- DUERKSEN J. D., HALVORSON H. The specificity of induction of beta-glucosidase in Saccharomyces cerevisiae. Biochim Biophys Acta. 1959 Nov;36:47–55. doi: 10.1016/0006-3002(59)90068-x. [DOI] [PubMed] [Google Scholar]
- EBERHART B., CROSS D. F., CHASE L. R. BETA-GLUCOSIDASE SYSTEM OF NEUROSPORA CRASSA. I. BETA-GLUCOSIDASE AND CELLULASE ACTIVITIES OF MUTANT AND WILD-TYPE STRAINS. J Bacteriol. 1964 Apr;87:761–770. doi: 10.1128/jb.87.4.761-770.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FRASER M. J., KAPLAN J. G. The alteration of intracellular enzymes. III. The effect of temperature on the kinetics of altered and unaltered yeast catalase. J Gen Physiol. 1955 Mar 20;38(4):515–547. doi: 10.1085/jgp.38.4.515. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HERMAN A., HALVORSON H. GENETIC CONTROL OF BETA-GLUCOSIDASE SYNTHESIS IN SACCHAROMYCES LACTIS. J Bacteriol. 1963 Apr;85:901–910. doi: 10.1128/jb.85.4.901-910.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HERMAN A., HALVORSON H. IDENTIFICATION OF THE STRUCTURAL GENE FOR BETA-GLUCOSIDASE IN SACCHAROMYCES LACTIS. J Bacteriol. 1963 Apr;85:895–900. doi: 10.1128/jb.85.4.895-900.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HU A. S., EPSTEIN R., HALVORSON H. O., BOCK R. M. Yeast beta-glucosidase: comparison of the physical-chemical properties of purified constitutive and inducible enzyme. Arch Biochem Biophys. 1960 Dec;91:210–218. doi: 10.1016/0003-9861(60)90492-6. [DOI] [PubMed] [Google Scholar]
- KAPLAN J. G. ACTION OF NON-PENETRATING HEAVY METALS ON THE CATALASE ACTIVITY OF YEAST CELLS. Nature. 1965 Jan 2;205:76–77. doi: 10.1038/205076a0. [DOI] [PubMed] [Google Scholar]
- KAPLAN J. G. THE REVERSION OF CATALASE DURING GROWTH OF YEAST IN ANAEROBIOSIS. J Gen Physiol. 1963 Sep;47:103–115. doi: 10.1085/jgp.47.1.103. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SIH C. J., NELSON N. M., McBEE R. H. Biological synthesis of cellobiose. Science. 1957 Nov 29;126(3283):1116–1117. doi: 10.1126/science.126.3283.1116. [DOI] [PubMed] [Google Scholar]