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Original Article

α-Amylase, Limit Dextrinase, and α-Glucosidase Enzymes in Barley and Malt

Pages 117-128 | Published online: 24 Jan 2010

References

  • Kneen E. A comparative study of the development of amylases in germinating cereals. Cereal Chem. 1944; 21: 304
  • Sandstedt R. M., Beckord O. C. Photomicrographic studies of wheat starch. II. Amylolytic enzymes and the amylase inhibitor of the developing wheat kernel. Cereal Chem. 1946; 23: 548
  • Duffus C. M. aL-Amylase activity in the developing barley grain and its dependence on gibberellic acid. Phytochemistry 1969; 8: 1205
  • MacGregor A. W., LaBerge D. E., Meredith W. O. S. Changes in barley kernels during growth and maturation. Cereal Chem. 1971; 48: 255
  • Bilderback D. E. Amylases in developing barley seeds. Plant Physiol. 1971; 48: 331
  • Stoddart J. L. Sequential changes in amylase isozymes during grain maturation in barley. Planta 1971; 97: 70
  • Grabar P., Daussant J. Study of barley and malt amylases by immunochemical methods. Cereal Chem. 1964; 41: 523
  • Allison M. J., Ellis R. P., Swanston J. S. Tissue distribution of α-amylase and phosphorylase in developing barley grain. J. Inst. Brew. 1974; 80: 488
  • MacGregor A. W., Gordon A. G., Meredith W. O. S. Site of α-amylase in developing barley kernels. J. Inst. Brew. 1974; 78, LacroixL. 1972
  • Brown H. T., Morris G. H. Researches on the germination of some of the Gramineae. J. Chem. Soc 1890; 57: 458, I
  • MacGregor A. W., LaBerge D. E., Meredith W. O. S. Separation of α- and β-amylase enzymes from barley malt by ion-exchange chromatography. Cereal Chem. 1971; 48: 490
  • Jones R. L., Jacobsen J. V. The role of the endoplasmic reticulum in the synthesis and transport of α-amylase in barley aleurone layers. Planta 1982; 156: 421
  • Frydenberg O., Nielsen G. Amylase isozymes in germinating barley seeds. Hereditas 1965; 54: 123
  • MacGregor A. W. A note on the formation of α-amylase in de-embryonated barley kernels. Cereal Chem. 1976; 54: 792
  • Momotani Y., Kato J. Effect of gibberellin A3 on in vivo and in vitro induction of α-amylase isozymes. Plant Growth Substances, J. Carr. Springer-Verlag, Berlin 1972; 352
  • Marchylo B. A., MacGregor A. W. Separation of barley malt α-amylase by chromatofocusing. Cereal Chem. 1983; 60: 311
  • Daussant J., Skakoun A. Immunochemical approaches to studies of isozyme regulation in higher plants. Isozymes: Current Topics in Biological and Medical Research 1981; 5: 175
  • Weselake R. J., MacGregor A. W., Hill R. D. An endogenous α-amylase inhibitor in barley kernels. Plant Physiol. 1983; 72: 809
  • Mundy J., Svendsen I., Hejgaard J. Barley α-amylase/subtilisin inhibitor. I. Isolation and characterization. Carlsberg Res. Commun. 1983; 81
  • Akazawa T., Miyata S. Biosynthesis and secretion of α-amylase and other hydrolases in germinating cereal seeds. Essays Biochem. 1982; 18: 40
  • Varner J. E. Giberellic acid-controlled synthesis of α-amylase in barley endosperm. Plant Physiol. 1964; 39: 413
  • Varner J. E., Ho D. T.-H. Hormones in Plant Biochemistry, J. Bonner, J. E. Varner. Academic Press, New York 1976; 713
  • Briggs D. E. Hormones and carbohydrate metabolism in germinating cereal grains. Biosynthesis, B. V. Milborrow. Academic Press, New York 1973; 219, its Control in Plants, Ed.
  • Jacobsen J. V., Higgins T. J. V. Characterization of the α-amylases synthesized by aleurone layers of Himalaya barley in response to gibberellic acid. Plant Physiol. 1647; 70, 1982
  • Rogers J. C. Two barley α-amylase gene families are regulated differently in aleurone cells. J. Biol. Chem. 1985; 260: 3731
  • Jones R. L., Jacobsen J. V. Calcium regulation of the secretion of α-amylase isoenzymes and other proteins from barley aleurone layers. Planta 1983; 158: 1
  • Jones R. L., Carbonell J. Regulation of the synthesis of barley aleurone α-amylase by gibberellic acid and calcium ions. Plant Physiol. 1984; 76, 213
  • Carbonell J., Jones R. L. A comparison of the effects of Ca and gibberellic acid on enzyme synthesis and secretion in barley aleurone. Physiol. Plant 1984; 63: 345
  • MacGregor A. W. Cereal α-amylases: synthesis and action pattern, in. Seed Proteins, J. Daussant, J. Mossé, J. Vaughan. Academic Press, London 1982
  • Akazawa T., Hara-Nishimura I. Topographic aspects of biosynthesis, extracellular secretion, and intracellular storage of proteins in plant cells. Annu. Rev. Plant Physiol. 1985; 36: 441
  • Aisien A. O., Palmer G. H. The sorghum embryo in relation to the hydrolysis of the endosperm during germination and seedling growth. J. Sci. Food Agric. 1983; 34: 113
  • Gibbons G. C., Nielsen E. B. New analysis in malting and brewing. J. Inst. Brew. 1983; 89: 8
  • MacGregor A. W., MacDougall F. H., Mayer C., Daussant J. Changes in levels of α-amylase components in barley tissues during germination and early seedling growth. Plant Physiol. 1984; 75: 203
  • Ranki H., Sopanen T. Secretion of α-amylase by the aleurone layer and the scutellum of germinating barley grain. Plant Physiol. 1984; 75: 710
  • MacGregor A. W., Marchylo B. A. α-Amylase components in excised, incubated barley embryos. J. Inst. Brew. 1986; 92: 159
  • Nicholls P. B. Environment, developing barley grain and subsequent production of α-amylase by the aleurone layer. J. E. Kruger, D. E. LaBerge. Westview Press, BoulderColo 1983; 147, Third International Symposium on Pre-Harvest Sprouting in Cereals
  • MacGregor A. W., Nicholls P. B., Dushnicky L. Endosperm degradation in barley kernels that synthesize α-amylase in the absence of embryos and exogenous gibberellic acid. Food Microstruct. 1983; 2: 13
  • MacGregor E. A., MacGregor A. W. Studies of cereal α-amylases using cloned DNA. CRC Crit. Rev. Biotechnol. 1987; 5
  • Bird R., Hopkins R. H. The action of some α-amylases on amylose. Biochem. J. 1954; 56: 86
  • Greenwood C. T., Milne E. A. Starch degrading and synthesizing enzymes: a discussion of their properties and action pattern. Adv. Carbohydr. Chem. 1968; 23: 281
  • MacGregor E. A., MacGregor A. W. The action of cereal α-amylase on solubilized starch and cereal starch granules, in. New Approaches to Research on Cereal Carbohydrates, R. D. Hill, L. Munck. Elsevier, Amsterdam 1985; 149
  • MacGregor E. A., MacGregor A. W. A model for the action of cereal α-amylases on amylose. Carbohydr. Res. 1985; 142: 223
  • Sandstedt R. M., Gates R. L. Raw starch digestion: a comparison of the raw starch digesting capabilities of the amylase systems from four α-amylase sources. Food Res. 1954; 19: 190
  • MacGregor A. W., Ballance D. L. Hydrolysis of large and small starch granules from normal and waxy barley cultivars by α-amylase from barley malt. Cereal Chem. 1980; 57: 397
  • Evers A. D., McDermott E. E. Scanning electron microscopy of wheat starch. II. Structure of granules modified by α-amylolysis—a preliminary report. Die Starke 1970; 22: 23
  • MacWilliam I. C., Harris G. Separation of limit dextrinase from R-enzyme and aspects of the activities of the separated enzymes. Arch. Biochem. Biophys. 1959; 84: 442
  • Hobson P. N., Whelan W. J., Peat S. The enzymic synthesis and degradation of starch. XIV. R-enzyme. J. Chem. Soc. 1951; 1451
  • Manners D. J., Hardie D. G. Studies on debranching enzymes. VI. The starch-debranching enzyme system of germinated barley. MBAA Tech. Q. 1977; 14: 120
  • Manners D. J. Debranching enzymes in plant tissues. Biochem. Soc. Trans. 1975; 3: 49
  • Manners D. J., Yellowlees D. Studies on debranching enzymes. I. The limit dextrinase activity of extracts of certain higher plants and commercial malts. J. Inst. Brew. 1973; 79: 377
  • Manners D. J. Some aspects of the metabolism of starch. Cereal Foods World 1985; 30: 722
  • Lenoir P., MacGregor A. W., Moll M., Daussant J. Identification of debranching enzyme from barley and malt by isoelectric focusing. C. R. Acad. Sc. Paris 1984, t. 298, Series III, 243
  • Yamada J. Purification of oat debranching enzyme and occurrence of inactive debranching enzyme in cereals. Agric. Biol. Chem. 1981; 45: 1013
  • Lee W. J., Pyler R. E. Barley malt limit dextrinase: varietal, environmental and malting effects. Am. Soc. Brew. Chem. 1984; 42: 11
  • Pratt G. W., Chappie T. W., Fahy M. J. Preparation of Malt High in α-1, 6-Hydrolase, U. S. Patent. 1981; 425: 1630
  • Hardie D. G. Control of carbohydrase formation by gibberellic acid in barley endosperms. Phytochemistry 1975; 14: 1719
  • Maeda I., Jimi N., Taniguchi H., Nakamura M. Purification of R-enzyme from malted barley and its role in in vitro digestion of barley starch granules. J. Jpn. Soc. Starch Sci. 1979; 26: 117
  • Manners D. J., Yellowlees D. Studies on carbohydrate metabolising enzymes. Die Stärke 1971; 23: 228, XXVI. The limit dextrinase from germinated barley
  • MacGregor A. W., Lenoir C. α-Glucosidase in barley and malt. Plant Physiol. (Suppl.) 1985; 77: 114
  • Watson T. G., Novellie L. Extraction of sorghum vulgare and hordeum vulgare α-glucosidase. Phytochemistry 1974; 13: 1037
  • Jorgensen O. B. Barley malt α-glucosidase. Acta Chem. Scand. 1965; 19: 1014, VI. Localisation and development during barley germination
  • Clutterbuck V. J., Briggs D. E. Enzyme formation and release by isolated barley aleurone layers. Phytochemistry 1973; 12: 537
  • Briggs D. E. Development of enzymes by barley embryos in vitro. J. Inst. Brew. 1962; 68: 470
  • Jorgensen O. B. Barley malt α-glucosidase. V. Degradation of starch and dextrins. Acta Chem. Scand. 1975; 18, 1964

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