Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1968 May;107(5):625–636. doi: 10.1042/bj1070625

Some properties of β-fructofuranosidases partially purified from Phaseolus vulgaris and Solanum tuberosum

G M Frost 1,*, R N Greenshields 1,†, F W J Teale 1
PMCID: PMC1198714  PMID: 16742583

Abstract

1. Soluble β-fructofuranosidases were purified 16-fold from French-bean-pod extracts and 35-fold from potato-tuber extracts. 2. The two enzymes had similar overall properties but differed from each other quantitatively in lability and reaction kinetics. 3. A non-diffusible inhibitor of β-fructofuranosidase was present in the potato-tuber extracts but was absent from the bean extracts. This non-competitive inhibitor was acid-labile. 4. The possible roles of imidazole, carboxyl and thiol groups in β-fructofuranosidase action are discussed, and the properties of the bean and potato enzymes are compared with published data for yeast, mould and grape-berry enzymes.

Full text

PDF
629

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ALLEN P. J., BACON J. S. Oligosaccharides formed from sucrose by fructose-transferring enzymes of higher plants. Biochem J. 1956 Jun;63(2):200–206. doi: 10.1042/bj0630200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Arnold W. N. A column method for enzymic characterization of coarse cellular fractions: application to insoluble beta-fructofuranosidase from grape. Arch Biochem Biophys. 1966 Feb;113(2):451–456. doi: 10.1016/0003-9861(66)90213-x. [DOI] [PubMed] [Google Scholar]
  3. Arnold W. N. Beta-fructofuranosidase from grape berries. Biochim Biophys Acta. 1965 Oct 25;110(1):134–147. doi: 10.1016/s0926-6593(65)80102-3. [DOI] [PubMed] [Google Scholar]
  4. BACON J. S. D., EDELMAN J. The carbohydrates of the Jerusalem artichoke and other Compositae. Biochem J. 1951 Jan;48(1):114–126. doi: 10.1042/bj0480114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BEALING F. J., BACON J. S. D. The action of mould enzymes on sucrose. Biochem J. 1953 Jan;53(2):277–285. doi: 10.1042/bj0530277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. COOPER R. A., GREENSHIELDS R. N. Sucrases in Phaseolus vulgaris. Nature. 1961 Aug 5;191:601–602. doi: 10.1038/191601b0. [DOI] [PubMed] [Google Scholar]
  7. Cooper R. A., Greenshields R. N. The partial purification and some properties of two sucrases of Phaseolus vulgaris. Biochem J. 1964 Aug;92(2):357–364. doi: 10.1042/bj0920357. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. DAHLQVIST A. Determination of maltase and isomaltase activities with a glucose-oxidase reagent. Biochem J. 1961 Sep;80:547–551. doi: 10.1042/bj0800547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. DIXON M. The effect of pH on the affinities of enzymes for substrates and inhibitors. Biochem J. 1953 Aug;55(1):161–170. doi: 10.1042/bj0550161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. EDELMAN J. Transfer reactions catalysed by some sucrase preparations. Biochem J. 1954 May;57(1):22–33. doi: 10.1042/bj0570022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GILLESPIE R. E., LARNER J. Gastrointestinal digestion of starch. II. Properties of the intestinal carbohydrases. J Biol Chem. 1956 Dec;223(2):709–726. [PubMed] [Google Scholar]
  12. HENDERSON R. W., MORTON R. K., RAWLINSON W. A. Oligosaccharide synthesis in the banana and its relationship to the transferase activity of invertase. Biochem J. 1959 Jun;72(2):340–344. doi: 10.1042/bj0720340. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hatch M. D., Sacher J. A., Glasziou K. T. Sugar Accumulation Cycle in Sugar Cane. I. Studies on Enzymes of the Cycle. Plant Physiol. 1963 May;38(3):338–343. doi: 10.1104/pp.38.3.338. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. KOSHLAND D. E., Jr, RAY W. J., Jr, ERWIN M. J. Protein structure and enzyme action. Fed Proc. 1958 Dec;17(4):1145–1150. [PubMed] [Google Scholar]
  15. Kivilaan A., Beaman T. C., Bandurski R. S. Enzymatic activities associated with cell wall preparations from corn coleoptiles. Plant Physiol. 1961 Sep;36(5):605–610. doi: 10.1104/pp.36.5.605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. LARNER J., GILLESPIE R. E. Participation of histidine in catalytic activity of intestinal carbohydrases. Arch Biochem Biophys. 1955 Sep;58(1):252–253. doi: 10.1016/0003-9861(55)90117-x. [DOI] [PubMed] [Google Scholar]
  17. METZENBERG R. L. The purification and properties of invertase of Neurospora. Arch Biochem Biophys. 1963 Mar;100:503–511. doi: 10.1016/0003-9861(63)90118-8. [DOI] [PubMed] [Google Scholar]
  18. Neumann N. P., Lampen J. O. Purification and properties of yeast invertase. Biochemistry. 1967 Feb;6(2):468–475. doi: 10.1021/bi00854a015. [DOI] [PubMed] [Google Scholar]
  19. RABEK V., MANSFIELD V. Gel filtration of protease inhibitors from potatoes. Experientia. 1963 Mar 15;19:151–152. doi: 10.1007/BF02171605. [DOI] [PubMed] [Google Scholar]
  20. ROREM E. S., SCHWIMMER S. Double pH optima of potato invertase. Experientia. 1963 Mar 15;19:150–151. doi: 10.1007/BF02171604. [DOI] [PubMed] [Google Scholar]
  21. RUCHTI J., MCLAREN A. D. ENZYME REACTIONS IN STRUCTURALLY RESTRICTED SYSTEMS V. FURTHER OBSERVATIONS ON THE KINETICS OF YEAST BETA-FRUCTOFURANOSIDASE (INVERTASE) ACTIVITY IN VISCOUS MEDIA. Enzymologia. 1964 Aug 15;27:185–198. [PubMed] [Google Scholar]
  22. RYAN C. A., BALLS A. K. An inhibitor of chymotrypsin from Solanum tuberosm and its behavior toward trypsin. Proc Natl Acad Sci U S A. 1962 Oct 15;48:1839–1844. doi: 10.1073/pnas.48.10.1839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Schwimmer S., Makower R. U., Rorem E. S. Invertase & invertase inhibitor in potato. Plant Physiol. 1961 May;36(3):313–316. doi: 10.1104/pp.36.3.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. THOMA J. A., WAKIM J., STEWART L. COMPARISON OF THE ACTIVE SITES OF ALPHA AND BETA AMYLASES. Biochem Biophys Res Commun. 1963 Aug 14;12:350–355. doi: 10.1016/0006-291x(63)90103-7. [DOI] [PubMed] [Google Scholar]
  25. TREVITHICK J. R., METZENBERG R. L. KINETICS OF THE INHIBITION OF NEUROSPORA INVERTASE BY PRODUCTS AND ANILINE. Arch Biochem Biophys. 1964 Aug;107:260–270. doi: 10.1016/0003-9861(64)90328-5. [DOI] [PubMed] [Google Scholar]
  26. WHITE J. W., Jr, SUBERS M. H. A glucose oxidase reagent for maltase assay. Anal Biochem. 1961 Aug;2:380–384. doi: 10.1016/0003-2697(61)90011-2. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES