Abstract
THE enzyme pullulanase1 is a bacterial R-enzyme in that it is capable of cleaving certain α 1→6 glucosidic bonds where these occur together with α 1→4 glucosidic bonds as in pullulan, starch and dextrins. The substrate specificity of this enzyme has recently been reported2 to embrace oligosaccharides and dextrins containing as few as two 1→4 linked α-D-glucopyranoside units in the ‘A’ chain and two such units in the ‘B’ chain. Thus, a tetra-saccharide linked 2 on 2 is the smallest known substrate for the hydrolytic action of this enzyme2.
Similar content being viewed by others
Article PDF
References
Bender, H., and Wallenfels, K., Biochem. Z., 334, 79 (1961).
Abdullah, M., Catley, B. J., Lee, E. T. C., Robyt, J., Wallenfels, K., and Whelan, W. J., Cereal Chem., 43, 111 (1966).
French, D., Pulley, A. O., Effenberger, J. A., Rougvie, M. A., and Abdullah, M., Arch. Biochem. Biophys., 111, 153 (1965).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
ABDULLAH, M., FRENCH, D. Reversible Action of Pullulanase. Nature 210, 200 (1966). https://doi.org/10.1038/210200a0
Issue Date:
DOI: https://doi.org/10.1038/210200a0
This article is cited by
-
On the cluster structure of amylopectin
Plant Molecular Biology (2022)
-
Preparation of maltotriose by hydrolyzing of pullulan with pullulanase
European Food Research and Technology (2009)
-
Glycosidases of turnip leaf tissues
Applied Biochemistry and Biotechnology (1994)
-
Purification and general biochemical properties of thermostable pullulanase fromBacillus stearothermophilus G-82
Applied Biochemistry and Biotechnology (1992)
-
Effect of carbon source and dissolved oxygen level on cell growth and pullulanase production byBacillus stearothermophilus G-82
World Journal of Microbiology & Biotechnology (1992)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.