PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2006 | 28 | 3 |

Tytuł artykułu

Presence of an alpha-amylase isozyme with high temperature optima in the wheat variety tolerant to high temperature at juvenile plant stage

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
In the present study α-amylase was partially purified from detached grains of five day old seedlings of two wheat (Triticum aestivum L.) varieties, showing differential responses to high temperature stress at seedling stage. A three step purification via ammonium sulphate precipitation, DEAE-cellulose column chromatography and gel filtration on Sephadex G-150 was employed. A single a-amylase was detected in the high temperature sensitive PBW-175 variety, while two isozymes namely, α-amylase-1 and α-amylase-2 were obtained in the relatively tolerant WL-711 variety. The pH optima of the three α-amylases were in 5.0-5.5 range and comparable to the cereal amylases. The temperature optima of PBW-175 α-amylase and α-amylase-1 of WL-711, which appeared to be the major isozyme of the variety, were same at 45 °C and also comparable to cereal amylases. On the other hand the optimum temperature for α-amylase-2 was high at 70 °C, which is unusual and not reported earlier for cereal amylases. The Km of PBW-175 α-amylase was lower than the Km values of WL-711 isozymes, this was well co-related with an overall high α-amylase activity detected in the detached grains of five day old seedlings of PBW-175 compared to WL-711. However WL-711 variety showed a better inherent seedling growth, vigour and EUE than PBW-175, may be because it had two α-amylase isozymes which could compensate for the higher enzyme activity detected in PBW-175. Moreover, the presence of α-amylase-2 in the grain of WL-711 having temperature optima of 70 °C, possibly rendered its seedlings tolerant to HS of 50 °C, while the seedlings of PBW-175 succumbed to this temperature shock.

Wydawca

-

Rocznik

Tom

28

Numer

3

Opis fizyczny

p.205-215,fig.,ref.

Twórcy

autor
  • Punjab Agricultural University, Ludhiana-141004, India

Bibliografia

  • Ainsworth C.C., Gale M.D. 1987. Enzymes structural genes and their exploitation in wheat genetics and breeding. In: Kruger JE, Lineback DR, Stautter CE (Eds.) Enzymes and their Role in Cereal Technology. AACC, St Paul Minnesota, USA pp 53-82.
  • Ashraf M., Saeed M.M., Qureshi M.J. 1994. Tolerance to high temperature in cotton (Gossypium hirsutum L.) at initial growth stages. Env Exp Bot., 34:275-283
  • Asthir B., Kaur A., Basra A.S. 1998a. Kinetic behaviour of soluble invertases may be connected with the differential heat sensitivity of two wheat genotypes. Acta Physiologiae Plantarum, 20: 285-289
  • Asthir B., Kaur A., Basra A.S. 1998b. Cultivar variation in heat stabiltty and kinetic properties of soluble invertases in wheat grains. Acta Physiologiae Plant arum, 20: 339-345
  • Bilderback D.E. 1974. Amylases from aleurone layers and starchy endosperm of bartey seeds. Plant Phystol- ogy, 53: 480-484
  • Blum A., Sinmena B. 1994. Wheat seed endosperm utilization under heat stress and its retation to thermot tolerancein autotrophic plant. Field Crops Research, 37: 185-191
  • Bog-Hansen T.C., Daussant J. 1974. Immunochemical quantitation of isozymes. a-Amylase isozymes in barley malt. Analytical Biochemistry, 61: 522-527
  • Duffus C., Rosie R. 1973. Starch hydrolysing enzymes in the developing barley grain. Planta, 109: 153-160
  • Fernandez T.J., Nicolas G. 1981. Purification and characterization of an a-amylase from the cotyledons of germinating lentils. Revista Espanol-de-Fisiologia, 37: 197-204
  • Ferreira A.G., Dietrich S.M.C., Handro W. 1979. Change in the metabolism of Araucaria angustifolia during the early phases of germination and growth Revista Brasileira de Botanica, 2: 67-71
  • Fincher G.B. 1989. Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains. Annual Review of Plant Physiology and Plant Molecular Biology, 40: 305-340
  • Frydenberg O., Nielsen G. 1966. Amylase isozymes in germinating barley seeds. Herediats, 54: 123-139
  • Greenwood C.T., MacGregor A.W. 1965. Isolation of a-amylase from barley and malted barley and a study of their properties and action patterns of the enzymes. Journal of the Institute of Breweries, 71: 405-417
  • Greenwood C.T., Milne E.A. 1968a. Studies on starch degrading enzymes. Part VII Properties and action pattern of the a-amylase from barley, oats, rye and wheat. Die Starke, 20: 101-107
  • Greenwood C.T., Milne E.A. 1968b. Studies on starch degrading enzymes. Part VIII. A comparison of a-amy- lases from different sources their properties and action pattern. Die Starke, 20: 139-150
  • Hall A. E. 1992. Breeding for heat tolerance.In: Janick J (ed) Plant Breeding Reviews, Vol 10 John Wiley Sons New York pp129-208
  • Huang N., Sutliff T.D., Litts J.C., Rodriguez R.L. 1990. Classification and characterization of the rice a-amylase multigene family. Plant Molecular Biology, 14: 655-668
  • Jacobsen J.V., Higgins T.J.V. 1982. Characterisation of the a-amylases synthe sized by aleurone layers of Himalaya barley in response to GA3. Plant Physiology, 70: 1647-1653
  • Jacobsen J.V., Scandalios J.G., Varner J.E. 1970. Multiple forms of amylase induced by gibberellic acid in isolated barley aleurone layers. Plant Physiology, 45: 367-371
  • Jones R.L., Carbonell J. 1984. Regulation of the synthesis of bartey aleurone alpha-amylase by gibberellic acid and calcium ions. Plant Physiology, 76: 213-218
  • Juliano B.O., Varner J.E. 1969. Enzymic degradation of starch granules in cotyledons of germinating peas. Plant Physiology, 44: 886-892
  • Koshiba T., Minamikawa T. 1981. Purificatiojn by affinity chromatography of α-amylase. A main amylase in cotyledons of germinating Vigna mungo seeds. Plant Cell Physiology, 22: 979-987
  • Levitt J. 1982. Response of plants to Environmental Stresses. Vol II, Academic Press New York, pp 497
  • Lineweaver H., Burk D. 1934. The determination of enzyme dissociation constants. Journal of American Chemistry Society, 56: 658-666
  • Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. 1951. Protein measurement with Folin phenol reagent. Journal of Biological Chemistry, 193: 265-275
  • MacGregor A.W. 1976. A note on the formation of the α-amylases in de-embryonated barley kernels. Cereal Chemistry, 53: 792-796
  • MacGregor A.W. 1977. Isolation, purification and electrophoretic properties of an α-amylase from malted barley. Journal of the Institute of Breweries, 83: 100-103
  • Maeda I., Kiribuchi S., Nakamura M. 1978. Digestion of barley starch granules by the combined action of α- and β-amylases purified from barley and barley malt. Agricultural Biological Chemistry, 42: 259-267
  • Mar S.S., Mori H., Lee J., Fuakuda K., Saburi W., Fukuhara A., Okuyama M., Chiba S., Kinura A. 2003. Purification, characterization and sequence analysis of two a-amyrase isoforms from azuki bean, Vigna angularis, showing different affinity towards β-cyclodextrin sepharose. Bioscience Biotechnology and Biochemistry, 67: 1080-1093
  • Marchylo B., Kruger J.E., Irvine G.N. 1976. α-Amylase from immature red spring wheat .I Purification and some chemical and physical properties. Cereal Chemistry, 53: 157-173
  • Masuda H., Takahashi T., Sugawara S. 1987. Purification and properties of starch hydrolysing enzyme in mature roots of sugarbeets. Plant Physiology, 84: 361-365
  • Meredith P., Jenkins L.D. 1973. Amylase activity of sprout-damaged, malted and immatured wheat. Cereal Chemistry, 50: 243-253
  • Mitsui T., Yamaguchi J., Akazawa T. 1996. Physicochemical and serological characterization of rice a-amylase isoforms and identification of their corresponding genes. Plant Physiology, 110: 1395-1404
  • Momotani Y., Kato J. 1970. Effect of gibberellin A3 on in vivo and in vitro induction of α-amylase isozymes. In: DJ Carr, (Ed). Plant Growth Substances. Springer- Verlag, Heidelberg, pp 352-355
  • Muthukrishnan S., Chandra G.R. 1988. Regulation of the expression of hydrolase genes in cereal seeds. Advances in Cereal Science and Technology Inc. St. Paul Minnesota, 129-159
  • Muthukrishnan S., Gill B.S., Swegle M., Chandra G.R. 1984. Structural genes for alpha-amylases are located on barley chromosomes 1 and 6. Journal of Biological Chemistry, 259: 13637-13639
  • Nirmala M., Muralikrishna G. 2003. Three α-amylases from malted finger mihet (Ragi, Eleusine cora- cana, Indaf-15) - Purification and partial characterization. Phytochemistry, 62: 21-30
  • Nyman B. 1971. Light, seed coat and gibberellic acid in relation to the amylase activity in germinating Scots pine seeds (Pinus sylvestris). Physiologiae Plantarum, 25: 112-117
  • Okamoto K., Akazawa T. 1979. Enzymic mechanism of starch breakdown in germinati ng rice seeds. Plant Physiology, 64: 337-340
  • Parkin K.L. 1993. In: Food Processing, third ed. Nagodawithona T and Reed G (Eds). Academic Press, New York, pp 7-36
  • Paulsen G.M. 1994. High temperature responses of crop plants. In: Boote KJ, Bennett JM, Sinclair T and Paulsen GM (Eds) Physiology and Determination of Crop Yield. American Society of Agronomy, Madison, pp 365-389
  • Reinero A., Balboa O., Cardemil L. 1983. Characterization of amylolytic activity of Araucaria araucana (Mol.) Koch germinating seeds. Plant Cell Physiology, 24: 456-495
  • Sprinz C. 1999. In: Food Chemishy. Belitz HD and Gross W (Eds), Springer Verlag, Berlin, Heidelberg, New York, pp 92-151
  • Subbarao K.V., Datta R., Sharma R. 1998. Amylases synthesis in scutellum and aleurone layer of maize seeds. Phytochemistry, 49: 657-666
  • Sun Z., Henson C.A. 1990. Degradation of native starch granules by barley α-glucosidases. Plant Physiology 94: 320-327
  • Sun Z., Henson C.A. 1991. A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme and α-glucosidase in starch degradation. Archives of Biochemistry and Biophysics, 284: 298-305
  • Swain R.R., Dekker E.E. 1966. Seed germination studies. I. Purification and properties of an α-amylase from cotyledons of germinating peas. Biochimica et Biophysica Acta, 122: 75-86
  • Tanaka Y., Akazawa T. 1970. α-Amylase isozymes in gibberellic acid treated barley half-seeds. Plant Physiology, 46: 586-591
  • Thoma J.A., Sparlin J.E., Dygert S. 1971. Plant and animal amylases. In: Boyer P. (Ed.) The Enzymes, vol. 7. Academic Press, New York, pp 115-189
  • Tkachuk R., Kruger J.E. 1974. Wheat α-amylases II. Physical Characterization. Cereal Chemistry, 51: 508-529
  • Vallee B.L., Stein E.A., Summerwell W.N., Fischer E.H. 1959. Metal content of α-amylases of various origins. Journal of Biological Chemistry, 234: 2901-2909

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-69127794-ffaf-4cee-a06b-7bdd78459688
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.