A Novel Maltopentaose-Producing Amylase as a Bread Antistaling Agent

  • Auh, Joong-Hyuck (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Lee, Su-Yong (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Yoo, Seung-Seok (Department of Culinary Science, Honam University) ;
  • Son, Hyun-Ju (Division of Food Science, College of Life and Environmental Sciences, Korea University) ;
  • Lee, Jae-Woo (Department of Food Science and Nutrition Management, Gimcheon College) ;
  • Lee, Sung-Joon (Division of Food Science, College of Life and Environmental Sciences, Korea University) ;
  • Kim, Young-Bae (Division of Food Science, College of Life and Environmental Sciences, Korea University) ;
  • Park, Kwan-Hwa (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University)
  • Published : 2005.10.31

Abstract

A maltopentaose-producing amylase (G5-amylase) from Bacillus megaterium KSM B-404 was applied to retard bread retrogradation. Retrogradation rates were determined by differential scanning calorimetry. Gel permeation chromatography determined changes in maltooligosaccharide composition and the molecular weight profiles of carbohydrate tractions. The baking process produced maltopentaose and maltotriose by the hydrolysis of starch molecules into small units. Amylose and amylopectin degradation as well as maltooligosaccharides produced by the enzyme were likely responsible for retarding starch retrogradation. Overall, addition of G5-amylase reduced the starch retrogradation rate, and was as effective as Novamyl(R), a commercial enzyme.

Keywords

References

  1. Cereal Chem. v.80 Starch hydrolyzing enzymes for retarding the staling of rice bread Gujral, H.S.;Haros, M.;Rosell, C.M. https://doi.org/10.1094/CCHEM.2003.80.6.750
  2. J. Agric. Food Chem. v.46 Cloning of novel maltooligosaccharide-producing amylases as anti staling agents for bread Min, B.C.;Yoon, S.H.;Kim, J.W.;Lee, Y.W.;Kim, Y.B.;Park, K.W. https://doi.org/10.1021/jf970755y
  3. J. Agric. Food Chem. v.50 Modulation of cyclizing activity and thermostability of cyclodextrin glucanotransferase and its application as an antistaling enzyme Lee, S.H.;Kim, Y.W.;Lee, S.;Auh, J.H.;Yoo, S.S.;Kim, T.J.;Kim, J.W.;Kim, S.T.;Rho, H.J.;Choi, J.H.;Kim, V.B.;Park, K.H. https://doi.org/10.1021/jf010928q
  4. Eur. Food Res. Technol. v.215 Effect of different carbohydrases on fresh bread texture Haros, M.;Rosell, C.M.;Benedito, C. https://doi.org/10.1007/s00217-002-0580-4
  5. J. Food Sci. v.59 Phospholipid hydrolysate and antistaling amylase effects on retrogradation of starch in bread Kweon, M.R.;Park, C.S.;Auh, J.H.;Cho, B.M.;Yang, N.S.;Park, K.H. https://doi.org/10.1111/j.1365-2621.1994.tb08193.x
  6. Food Chem. v.52 Emulsifier in bread making Stampfli, L.;Nerste, B. https://doi.org/10.1016/0308-8146(95)93281-U
  7. J. Cereal Sci. v.28 Crumb firming kinetics of wheat breads with antistaling additives Armero, A.;Collar, C. https://doi.org/10.1006/jcrs.1998.0190
  8. Cereal Food World v.35 Developments in enzymes for retarding staling of baked goods Hebeda, R.E.;Bowles, L.K.;Teague, W.M.
  9. Food Technol. v.44 Antistaling enzymes for baked goods Boyle, P.J.;Hebeda, R.E.
  10. Cereal Chem. v.68 A mechanism of bread firming. II. Role of starch hydrolyzing enzymes Martin, M.L.;Hoseney, R.C.
  11. Cereal Chem. v.71 Water soluble dextrins from ${\alpha}-amylase$ treated bread and their relationship to bread firming Akers, A.A.;Hoseney, R.C.
  12. Eur. Food Res. Technol. v.212 Effect of low molecular weight dextrins on gelatinization and retrogradation of starch Duran, E.;Leon, A.;Barber, B.;de Barber, C. https://doi.org/10.1007/s002170000205
  13. Z Lebensm. Unters. Forsch. A. v.205 Firming of starch gels and amylopectin retrogradation as related to dextrin production by ${\alpha}-amylase$ Leon, A.;Duran, E.;de Barber, C. https://doi.org/10.1007/s002170050139
  14. Expression of the amylase gene from B. megaterium KSM B-404 in B. subtilis LKS88 and the maltopentaose production Son, H.J.
  15. Kor. J. Microbial. Biotechnol. v.30 Purification and characterization of maltopentaose-producing amylase from Bacillus megaterium KSM B-404 Park, J.W.;Kim, B.J.;Lee, J.W.;Kim, Y.B.
  16. Anal. Chem. v.31 Use of dinitrosalicylic acid reagent for determination of reducing sugar Miller, G.L. https://doi.org/10.1021/ac60147a030
  17. Nature v.227 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Laemmli, U.K. https://doi.org/10.1038/227680a0
  18. Starch v.42 Changes in carbohydrate tractions in enzymesupplemented bread and the potential relationship to staling Lin, W.;Linback, D.R. https://doi.org/10.1002/star.19900421005
  19. Agric. Biol. Chem. v.49 Characterization of maltopentaose-producing bacterium and its cultural conditions Yoshigi, N.;Chikano, T.;Kamimura, M. https://doi.org/10.1271/bbb1961.49.2379
  20. J. Agric. Food Chem. v.52 Effects of ${\alpha}-amylase$ from sources on the firming of concentrated wheat starch gels: Relationship to bread staling Palacios, H.R.;Schwarz, P.B.;Appolonia, B.L.D. https://doi.org/10.1021/jf030384n
  21. Carbohydr. Polym. v.51 The influence of various small plasticizers and malto-oligosaccharides on the retrogradation of (partly) gelatinized starch Smits, A.L.M.;Kruiskamp, P.H.;van Soest, J.J.G.;Vilegenthart, J.F.G. https://doi.org/10.1016/S0144-8617(02)00206-0
  22. Carbohydr. Res. v.325 The conformation of ${\alpha}-(1.4)-linked$ glucose oligomers from maltose to maltoheptaose and shortchain amylose in solution Sugiyama, H.;Nitta, T.;Horii, M.;Motohashi, K.;Sakai, J.;Usui, T.;Hisamichi, K.;Ishiyama, J. https://doi.org/10.1016/S0008-6215(99)00310-9
  23. Cereal Chem. v.50 Reactions of oligosaccharides. III. Hygroscopic properties Donnelly, B.J.;Fruin, J.C.;Scallet, B.L.
  24. Food Sci. Biotechnol. v.14 Estimating the glass transition of oligosaccharides mixtures through the state diagram Auh, J.H.;Park, K.H.
  25. Polymer v.34 A study of the glass transition of amylopectin-sugar mixtures Kalichevsky, M.T.;Jaroszkiewicz, E.M.;Blanshard, J.M.Y. https://doi.org/10.1016/0032-3861(93)90088-R
  26. Carbohydr. Res. v.135 The roles of amylose and amylopectin in the gelatinization and retrogradation of starch Miles, M.J.;Morris, V.J.;Orford, P.D.;Ring, S.G. https://doi.org/10.1016/S0008-6215(00)90778-X