Hostname: page-component-78c5997874-j824f Total loading time: 0 Render date: 2024-11-15T19:19:06.279Z Has data issue: false hasContentIssue false

Endo-β-mannanase and β-mannosidase activities in rice grains during and following germination, and the influence of gibberellin and abscisic acid

Published online by Cambridge University Press:  22 February 2007

Aoxue Wang*
Affiliation:
Department of Molecular and Cellular Biology, Axelrod Building, University of Guelph, Guelph, Ontario, N1G 2W1, Canada
Xiaofeng Wang
Affiliation:
College of Life Sciences, South China Agricultural University, Guangzhou, China, 510642
Yanfang Ren
Affiliation:
College of Life Sciences, South China Agricultural University, Guangzhou, China, 510642
Xuemei Gong
Affiliation:
Department of Molecular and Cellular Biology, Axelrod Building, University of Guelph, Guelph, Ontario, N1G 2W1, Canada
J. Derek Bewley*
Affiliation:
Department of Molecular and Cellular Biology, Axelrod Building, University of Guelph, Guelph, Ontario, N1G 2W1, Canada
*
*Correspondence Fax: +1 519 837 1075, Email: [email protected]
*Correspondence Fax: +1 519 837 1075, Email: [email protected]

Abstract

Grains of indica rice (Oryza sativa cv. Peiza 67) exhibit an increase in endo-β-mannanase activity, mostly after the completion of germination. According to tissue blots, the initial increase occurs in association with the embryo, and possibly the scutellum, although the largest sustained increase in activity is in the peripheral regions of the endosperm. The aleurone layer, being the only living region of the endosperm, is presumably the site of synthesis and secretion of the enzyme into the non-living, starch-laden region. β-Mannosidase activity is low throughout germination and subsequent seedling growth, particularly in the endosperm regions. Its activity profile does not mimic that of endo-β-mannanase. In the intact grain, gibberellin (GA) causes a relatively small increase in endo-β-mannanase activity, while abscisic acid (ABA) causes a large decrease; this inhibition is overcome to a considerable extent when GA is supplied along with ABA. β-Mannosidase activity is little affected by either GA or ABA. Embryoless half-grains imbibed in water exhibit only a small increase in endo-β-mannanase activity with time of imbibition, showing the necessity for a stimulus from the embryo for this to occur. Incubating half-grains in the presence of GA results in a large increase in enzyme activity; ABA reduces the amount of activity compared to the water controls. GA is capable of reversing the inhibitory effect of ABA with respect to endo-β-mannanase activity. As in the intact grains, β-mannosidase activity in the half-grains is unaffected by either GA or ABA. It is concluded that the major site for the production of endo-β-mannanase activity is the aleurone layer, and this event is influenced by the presence of the embryo; in the absence of the latter, the increase in enzyme activity is stimulated by GA. β-Mannosidase activity is low throughout germination and post-germination, it is not influenced by GA and ABA, and thus its activity is not regulated in a coordinated manner with that of endo-β-mannanase.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2005

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Bewley, J.D. (1997) Breaking down the walls – a role for endo-β-mannanase in release from seed dormancy? Trends in Plant Science 2, 464469.Google Scholar
Bewley, J.D. and Black, M. (1994) Seeds: Physiology of development and germination (2nd edition) New York. Plenum Press.CrossRefGoogle Scholar
Bewley, J.D. and Reid, J.S.G. (1985) Mannans and glucomannans. pp. 289304in Dey, P.M.;Dixon, R.A. (Eds) Biochemistry of storage carbohydrates in green plants. London, Academic Press.Google Scholar
Bourgault, R. and Bewley, J.D. (2002) Gel diffusion assays for endo-β-mannanase and pectin methylesterase can underestimate enzyme activity due to proteolytic degradation. A remedy. Analytical Biochemistry 300, 8793.CrossRefGoogle ScholarPubMed
DeMason, D.A., Sexton, R., Gorman, M. and Reid, J.S.G. (1985) Structure and biochemistry of endosperm breakdown in date palm (Phoenix dactylifera) seeds. Protoplasma 126, 159167.CrossRefGoogle Scholar
Dirk, L.M.A., Griffen, A.M., Downie, B. and Bewley, J.D. (1995) Multiple isozymes of endo-β-mannanase in dry and imbibed seeds. Phytochemistry 40, 10451056.Google Scholar
Dirk, L.M.A., van der, Krol A.R., Vreugdenhil, D., Hilhorst, H.W.M. and Bewley, J.D. (1999) Galactomannan, soluble sugar, and starch mobilization following germination of Trigonella foenum-graecum seeds. Plant Physiology and Biochemistry 37, 4150.CrossRefGoogle Scholar
Downie, B., Hilhorst, H.W.M. and Bewley, J.D. (1997) Endo-β-mannanase activity during dormancy alleviation and germination of white spruce (Picea glauca [Moench.] Voss.) seeds. Physiologia Plantarum 101, 405415.CrossRefGoogle Scholar
Fincher, G.B. and Stone, B.A. (1974) Some chemical and morphological changes induced by gibberellic acid in embryo-free wheat grain. Australian Journal of Plant Physiology 1, 297311.Google Scholar
Gibbons, G.C. (1979) On the localisation and transport of α-amylase during germination and early seedling growth of Hordeum vulgare. Carlsberg Research Communications 44, 353366.CrossRefGoogle Scholar
McCleary, B.V. and Matheson, N.K. (1975) Galactomannan structure and β-mannanase and β-mannosidase activity in germinating legume seeds. Phytochemistry 14, 11871194.CrossRefGoogle Scholar
Mo, B. and Bewley, J.D. (2002) β-Mannoside mannohydrolase (E.C.3.2.1.25) activity during and following germination of tomato (Lycopersicon esculentum Mill.) seeds. Purification, cloning and characterization. Planta 215, 141152.CrossRefGoogle Scholar
Mo, B. and Bewley, J.D. (2003) The relationship between β-mannosidase and endo-β-mannanase activities in tomato seeds during and following germination. A comparison of seed populations and individual seeds. Journal of Experimental Botany 54, 25032510.CrossRefGoogle ScholarPubMed
Murata, T., Akazawa, T. and Fukuchi, S. (1968) Enzymic mechanism of starch breakdown in germinating rice seeds. I. An analytical study. Plant Physiology 43, 18991905.Google Scholar
Okamoto, K. and Akazawa, T. (1979) Enzymic mechanisms of starch breakdown in germinating rice seeds. 7. Amylase formation in the epithelium. Plant Physiology 63, 336340.CrossRefGoogle ScholarPubMed
Ouellette, B.F.F. and Bewley, J.D. (1986) β-Mannoside mannohydrolase and the mobilization of the endosperm cell wall of lettuce seeds, cv. Grand Rapids. Planta 169, 333338.CrossRefGoogle ScholarPubMed
Palmiano, E.P. and Juliano, B.O. (1972) Biochemical changes in the rice grain during germination. Plant Physiology 49, 751756.CrossRefGoogle ScholarPubMed
Reid, J.S.G. (1985) Galactomannans. pp. 265288in Dey, P.M.;Dixon, R.A. (Eds) Biochemistry of storage carbohydrates in green plants. London, Academic Press.Google Scholar
Reid, J.S.G. and Meier, H. (1973) Enzymic activities and galactomannan mobilization in germinating seeds of fenugreek (Trigonella foenum-graecum Leguminosae). Secretion of α-galactosidase and β-mannosidase by the aleurone layer. Planta 112, 301308.CrossRefGoogle Scholar
Shibuya, N. and Iwasaki, T. (1978) Polysaccharides and glycoproteins in the rice endosperm cell wall. Agricultural and Biological Chemistry 42, 22592266.Google Scholar
Taiz, L. and Jones, R.L. (1970) Gibberellic acid, β-1,3-glucanase and the cell walls of barley aleurone layers. Planta 92, 7384.Google Scholar