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. 1976 Aug 1;157(2):381–387. doi: 10.1042/bj1570381

The beta-glucosidase in the gut contents of the snail Achatina achatina.

G M Umezurike
PMCID: PMC1163863  PMID: 9070

Abstract

1. The enzyme beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) from the gut contents of active Achatina achatina exists in two molecular forms, beta-glucosidase C (mol.wt. about 82000) and D (mol.wt. about 41000). 2. Only the lower-molecular-weight species was found in the gut contents of aestivating snails or in extracts from their digestive glands and washed gut walls. 3. On re-activation of some aestivating snails, betion of ATP and Mg2+ to the isolated gut contents or to extracts from washed gut walls led to the formation of higher-molecular-weight forms of the enzyme, beta-glucosidase A (mol.wt. about 329000) and beta-glucosidase B (mol.wt. about 165000). 5. All these forms of the enzyme have similar pH optimum (pH 5.0-5.6). 6. The Michaelis constants (Km) and heat stability of the enzyme increased with increasing molecular complexity.

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Selected References

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  1. Abrahams H. E., Robinson D. Beta-D-glucosidases and related enzymic activities in pig kidney. Biochem J. 1969 Mar;111(5):749–755. doi: 10.1042/bj1110749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Fleming L. W., Duerksen J. D. Evidence for multiple molecular forms of yeast beta-glucosidase in a hybrid yeast. J Bacteriol. 1967 Jan;93(1):142–150. doi: 10.1128/jb.93.1.142-150.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fleming L. W., Duerksen J. D. Purification and characterization of yeast beta-glucosidases. J Bacteriol. 1967 Jan;93(1):135–141. doi: 10.1128/jb.93.1.135-141.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. GALLI D. R., GIESE A. C. Carbohydrate digestion in a herbivorous snail. Tegula funebralis. J Exp Zool. 1959 Apr;140:415–440. doi: 10.1002/jez.1401400305. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Han Y. W., Srinivasan V. R. Purification and characterization of beta-glucosidase of Alcaligenes faecalis. J Bacteriol. 1969 Dec;100(3):1355–1363. doi: 10.1128/jb.100.3.1355-1363.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Horikoshi K., Ikeda Y. Studies on the spore coats of aspergillus oryzae. II. Conidia coat-bound beta-glucosidase. Biochim Biophys Acta. 1965 Nov 1;101(3):352–357. doi: 10.1016/0926-6534(65)90014-x. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Legler G. Labelling of the active centre of a beta-glucosidase. Biochim Biophys Acta. 1968 Mar 25;151(3):728–729. doi: 10.1016/0005-2744(68)90033-8. [DOI] [PubMed] [Google Scholar]
  13. Li L. H., Flora R. M., King K. W. Individual roles of cellulase components derived from Trichoderma viride. Arch Biochem Biophys. 1965 Aug;111(2):439–447. doi: 10.1016/0003-9861(65)90207-9. [DOI] [PubMed] [Google Scholar]
  14. MAHADEVAN P. R., EBERHART B. ARYL BETA-GLUCOSIDASE OF SOME NEUROSPORA STRAINS. Biochim Biophys Acta. 1964 Jul 15;90:214–215. doi: 10.1016/0304-4165(64)90147-3. [DOI] [PubMed] [Google Scholar]
  15. Marchin G. L., Duerksen J. D. Purification of beta-glucosidase from Saccharomyces lactis strain Y-123. J Bacteriol. 1968 Oct;96(4):1181–1186. doi: 10.1128/jb.96.4.1181-1186.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Marchin G. L., Duerksen J. D. Purification of beta-glucosidase from Saccharomyces lactis strains Y-14 and Y-1057A. J Bacteriol. 1968 Oct;96(4):1187–1190. doi: 10.1128/jb.96.4.1187-1190.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. PARNAS I. The cellulolytic activity in the snail Levantina hierosolyma Boiss. J Cell Comp Physiol. 1961 Oct;58:195–201. doi: 10.1002/jcp.1030580211. [DOI] [PubMed] [Google Scholar]
  18. ROBINSON D. The fluorimetric determination of beta-glucosidase: its occurrence in the tissues of animals, including insects. Biochem J. 1956 May;63(1):39–44. doi: 10.1042/bj0630039. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Robinson D., Price R. G., Dance N. Rat-urine glycosidases and kidney damage. Biochem J. 1967 Feb;102(2):533–538. doi: 10.1042/bj1020533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Robinson D., Price R. G., Dance N. Separation and properties of beta-galactosidase, beta-glucosidase, beta-glucuronidase and N-acetyl-beta-glucosaminidase from rat kidney. Biochem J. 1967 Feb;102(2):525–532. doi: 10.1042/bj1020525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Umezurike G. M. The purification and properties of extracellular beta-glucosidase from Botryodiplodia theobromae Pat. Biochim Biophys Acta. 1971 Feb 10;227(2):419–428. doi: 10.1016/0005-2744(71)90073-8. [DOI] [PubMed] [Google Scholar]
  22. Umezurike G. M. The subunit structure of beta-glucosidase from Botryodiplodia theobromae Pat. Biochem J. 1975 Feb;145(2):361–368. doi: 10.1042/bj1450361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wood T. M. The cellulase of Fusarium solani. Purification and specificity of the -(1-4)-glucanase and the -D-glucosidase components. Biochem J. 1971 Feb;121(3):353–362. doi: 10.1042/bj1210353. [DOI] [PMC free article] [PubMed] [Google Scholar]

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