DOI QR코드

DOI QR Code

Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11

  • Matsubara, Takayoshi (Laboratory of Enzyme Chemistry, Graduate School of Science, Osaka City University) ;
  • Ammar, Youssef Ben (Laboratory of Enzyme Chemistry, Graduate School of Science, Osaka City University) ;
  • Anindyawati, Trisanti (R&D Center for Biotechnology, Indonesian Institute of Science (LIPI)) ;
  • Yamamoto, Satoru (Laboratory of Enzyme Technology, Department of Biotechnology, Faculty of Life Science & Biotechnology, Fukuyama University) ;
  • Ito, Kazuo (Laboratory of Enzyme Chemistry, Graduate School of Science, Osaka City University) ;
  • Iizuka, Masaru (Laboratory of Enzyme Chemistry, Graduate School of Science, Osaka City University) ;
  • Minamiura, Noshi (Laboratory of Enzyme Chemistry, Graduate School of Science, Osaka City University)
  • Published : 2004.07.31

Abstract

Raw-starch-digesting $\alpha$-amylase (Amyl III) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT-11 using wheat bran in the medium. The purified Amyl III digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl III were maltotriose and maltose, although a small amount of glucose was produced. Amyl III acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl III on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl III and GA I was observed for the digestion of raw starch granules.

Keywords

References

  1. Akabori, S., Ikenaka, T. and Hagihara, B. (1954) Isolation of crystalline taka-amylase A from 'Takadiastase Sankyo'. J. Biochem. 41, 577-582.
  2. Anindyawati, T., Melliawati, R., Ito, K., Iizuka, M. and Minamiura, N. (1998a) Three different types of $\alpha$-amylases from Aspergillus awamori KT-11: Their purifications, properties and specificities. Biosci. Biotechnol. Biochem. 62, 1351-1357. https://doi.org/10.1271/bbb.62.1351
  3. Anindyawati, T., Ann, Y. G., Ito, K., Iizuka, M. and Minamiura, N. (1998b) Two kinds of novel $\alpha$-glucosidases from Aspergillus awamori KT-11: Their purifications, properties and specificities. J. Ferment. Bioeng. 85, 465-469. https://doi.org/10.1016/S0922-338X(98)80063-9
  4. Arai, M., Koyano, T., Ozawa, H., Minoda, Y. and Yamada, K. (1968) Acid-stable $\alpha$-amylase of black aspergilli. Part IV. Some physicochemical propreties. Agric. Biol. Chem. 32, 507-513. https://doi.org/10.1271/bbb1961.32.507
  5. Bhella, R. S. and Altosaar, I. (1984) Purification and some properties of the extracellular $\alpha$-amylase from Aspergillus awamori. Can. J. Microbiol. 31, 149-153.
  6. Fischer, E. H. and Montmollin, R. D. (1951) Crystallization of the $\alpha$-amylase of Aspergillus oryzae. Nature 168, 606-607. https://doi.org/10.1038/168606a0
  7. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage $T_{4}$. Nature 227, 680-685. https://doi.org/10.1038/227680a0
  8. Miah, M. N. N. and Ueda, S. (1977) Multiplicity of glucoamylase of Aspergillus oryzae. Starch/Starke 29, 235-239. https://doi.org/10.1002/star.19770290706
  9. Mikami, S., Iwano, K., Shiinoki, S. and Shimada, T. (1987) Purification and some properties of acid-stable $\alpha$-amlase from shochu koji (Aspergillus kawachii). Agric. Biol. Chem. 51, 2495-2501. https://doi.org/10.1271/bbb1961.51.2495
  10. Somogyi, N. (1952) Notes on sugar determination. J. Biol. Chem. 195, 19-23.
  11. Ueda, S., Ohba, R. and Kano, S. (1974) Fractionation of the glucoamylase system from black-koji mold and the effects of adding isoamylase and $\alpha$-amylase on amylolysis by the glucoamylase fraction. Starch/Starke, 26, 374-378. https://doi.org/10.1002/star.19740261104
  12. Ueda, S. (1981) Fungal glucoamylases and raw starch digestion. Trends Biochem. Sci. 6, 89-90. https://doi.org/10.1016/0968-0004(81)90032-3
  13. Yamamoto, T. (1995) Raw starch digesting amylolytic enzymes; in Enzyme Chemistry and Molecular Biology of Amylases and Related Enzymes, The Amylase Society of Japan (ed.), pp 40-45, CRC Press, Tokyo, Japan.
  14. Yamazaki, Y., Suzuki, Y. and Ozawa, J. (1977) Three forms of $\alpha$-glucosidase and a glucoamylase form Aspergillus awamori. Agric. Biol. Chem. 41, 2149-2161.

Cited by

  1. Characterization and application of a detergent-stable alkaline α-amylase from Bacillus subtilis strain AS-S01a vol.50, pp.1, 2012, https://doi.org/10.1016/j.ijbiomac.2011.10.026
  2. Sedimentation field flow fractionation monitoring of bimodal wheat starch amylolysis vol.1129, pp.2, 2006, https://doi.org/10.1016/j.chroma.2006.06.104
  3. Gene Sequence, Bioinformatics and Enzymatic Characterization of α-Amylase from Saccharomycopsis fibuligera KZ vol.29, pp.5, 2010, https://doi.org/10.1007/s10930-010-9260-6
  4. Physicochemical Property of Starch-Soluble Dietary Fiber Conjugates and Their Resistance to Enzymatic Hydrolysis vol.18, pp.11, 2015, https://doi.org/10.1080/10942912.2014.968785
  5. Spherulitic self-assembly of debranched starch from aqueous solution and its effect on enzyme digestibility vol.55, 2016, https://doi.org/10.1016/j.foodhyd.2015.11.027
  6. Immobilization of a saccharifying raw starch hydrolyzing enzyme on functionalized and non-functionalized sepa beads vol.78, 2012, https://doi.org/10.1016/j.molcatb.2012.01.019
  7. Sedimentation field flow fractionation monitoring of rice starch amylolysis vol.1093, pp.1-2, 2005, https://doi.org/10.1016/j.chroma.2005.07.084
  8. Cloning, expression, and purification of insect (Sitophilus oryzae) alpha-amylase, able to digest granular starch, in Yarrowia lipolytica host vol.99, pp.6, 2015, https://doi.org/10.1007/s00253-014-6314-2
  9. Amylolytic activity and its parametric optimization of an endophytic bacterium Bacillus subtilis with an ethno-medicinal origin vol.70, pp.3, 2015, https://doi.org/10.1515/biolog-2015-0047
  10. An overview on advances of amylases production and their use in the production of bioethanol by conventional and non-conventional processes vol.1, pp.4, 2011, https://doi.org/10.1007/s13399-011-0023-1
  11. Improving the Catalytic Performance of a Talaromyces leycettanus α-Amylase by Changing the Linker Length vol.65, pp.24, 2017, https://doi.org/10.1021/acs.jafc.7b00838
  12. Recent Advances in Microbial Raw Starch Degrading Enzymes vol.160, pp.4, 2010, https://doi.org/10.1007/s12010-009-8579-y
  13. Valorization of Residual Agroindustrial Cakes by Fungal Production of Multienzyme Complexes and Their Use in Cold Hydrolysis of Raw Starch vol.2, pp.3, 2011, https://doi.org/10.1007/s12649-011-9075-5
  14. Improvement of the RT-CaCCO Process for Efficient Glucose Recovery from Starch-rich Whole-crop Rice vol.59, pp.4, 2012, https://doi.org/10.5458/jag.jag.JAG-2012_005
  15. Impact of the Soak and the Malt on the Physicochemical Properties of the Sorghum Starches vol.11, pp.8, 2010, https://doi.org/10.3390/ijms11083002
  16. Applications of a high maltose forming, thermo-stable α-amylase from an extremely alkalophilic Bacillus licheniformis strain AS08E in food and laundry detergent industries vol.77, 2013, https://doi.org/10.1016/j.bej.2013.06.012
  17. A novel thermostable, acidophilic α-amylase from a new thermophilic “Bacillus sp. Ferdowsicous” isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization vol.46, pp.3, 2010, https://doi.org/10.1016/j.ijbiomac.2010.01.013
  18. EngineeringSaccharomyces cerevisiaefor direct conversion of raw, uncooked or granular starch to ethanol vol.35, pp.3, 2015, https://doi.org/10.3109/07388551.2014.888048
  19. The Effect of Soaking with Wooden Ash and Malting upon Some Nutritional Properties of Sorghum Flour Used for Impeke, a Traditional Burundian Malt-Based Sorghum Beverage vol.10, pp.11, 2011, https://doi.org/10.1016/S1671-2927(11)60180-6
  20. Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches vol.9, pp.1, 2016, https://doi.org/10.1186/s13068-016-0604-0
  21. Efficient hydrolysis of raw starch and ethanol fermentation: a novel raw starch-digesting glucoamylase from Penicillium oxalicum vol.9, pp.1, 2016, https://doi.org/10.1186/s13068-016-0636-5
  22. Identification and Manipulation of Subsite Structure and Starch Granule Binding Site in Plant .ALPHA.-Amylase vol.53, pp.1, 2006, https://doi.org/10.5458/jag.53.51