Characterization of glucoamylase from Lactobacillus amylovorus ATCC 33621

@article{James2004CharacterizationOG,
  title={Characterization of glucoamylase from Lactobacillus amylovorus ATCC 33621},
  author={Jennylynd A. James and Byong Hoon Lee},
  journal={Biotechnology Letters},
  year={2004},
  volume={18},
  pages={1401-1406}
}
An intracellular glucoamylase, purified from Lactobacillus amylovorus, reacted selectively with polysaccharides. Kinetic studies indicated low affinity for maltose and maltotriose (Km 58 g/ml and 178 g/ml) and higher affinity for starch and dextrin (Km 0.01 g/ml and 0.02 g/ml). Glucoamylase was inhibited almost 50% by 10 mM glucose. Cu2+ and Pb2+ inhibited glucoamylase at 1.0 mM but EDTA and other metal chelators had no effect on the enzyme activity. Acarbose and Tris inhibited the enzyme by 84… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-5 of 5 references

Agric

  • H.
  • Biol. Chem. 49, 2521-2523. Bender, H. (1981). fur…
  • 1985
Highly Influential
4 Excerpts

FEMS Microbial

  • A. Science Publishers. Ghosh, B. S. Chatterjee, A. Das
  • Left. 66, 345-349. Harris, E.M.S., Aleshin, A.E…
  • 1990

Carbohydrate Res

  • J. Abe, K. Nakajima, H. Nagano, S. Hizukuri
  • 175, 85-92. Ashikari, T., Nakamura, N., Tanaka, Y…
  • 1988
2 Excerpts

Anal

  • E.K., N. M. Goeke, B. J. Olson, D. C. Klenk
  • Biochem. 150, 76-85. Specka, U., Mayer, F. and…
  • 1985

Wisconsin: Master Brewers Association of the Americas

  • Broderick, ed
  • 1983

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