Inhibition of glucosidases and galactosidases by polyols |
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| Authors: | M V Kelemen W J Whelan |
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| Affiliation: | 1. Department of Plant Pathology, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115-111, Tehran, Iran;2. Dryland Agricultural Research Institute, Agricultural Research, Education & Extension Organization (ARREO), Maragheh, Iran;3. Seed & Plant Improvement Institute, Agricultural Research, Education & Extension Organization (ARREO), P.O. Box 31585-4119, Karaj, Iran;4. Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, Iran;5. Department of Plant Pathology, Faculty of Agricultural Sciences and Engineering, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran;6. Laboratory of Phytopathology, Wageningen University and Research, 6700AA Wageningen, The Netherlands;7. Wageningen University and Research, Wageningen Plant Research, P.O. Box 16, 6700AA Wageningen, The Netherlands;1. Research Unit for Tissue Regeneration, Repair, and Reconstruction, Division of Plastic, Aesthetic and Reconstructive Surgery, Department of Surgery, Medical University of Graz, Graz, Austria;2. Institute of Cell Biology, Histology and Embryology, Medical University of Graz, Graz, Austria;3. Division of Biomedical Research, Medical University of Graz, Graz, Austria;1. College of Life Sciences, Hebei Agricultural University, Baoding 071001, P.R. China;2. Quantum Design China, Beijing 100027, P.R. China;3. Beijing Protein Innovation Co., Ltd., Beijing 101318, P.R. China |
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| Abstract: | The hydrolyses of p-nitrophenyl α- and β-galactosides and p-nitrophenyl α- and β-glucosides by an α-galactosidase from Aspergillus fumigatis, an α-glucosidase from germinated barley, and almond β-glucosidase, which also has β-galactosidase activity, have been examined in the presence of glycerol, erythritol, d-threitol, ribitol, xylitol, d-arabitol and dl-butan-1,2,4-triol. The α-galactosidase was best inhibited by d-threitol, while the α-glucosidase was best inhibited by erythritol. Both inhibitions were competitive. The inhibitory character of these compounds may be attributed to their similarity in structure with the glycon of the substrate between C-3, C-4, C-5, and C-6. The β-glucosidase was best inhibited by erythritol, demonstrating a similarity of action between α- and β-glucosidases. However, the best inhibitor of β-galactosidase was erythritol. This observation confirmed the view that in almond emulsin, the glucosidase and galactosidase activities are found in the same enzyme. |
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