Purification and some properties of a starch debranching enzyme ofHendersonula toruloidea.

@article{Odibo1992PurificationAS,
  title={Purification and some properties of a starch debranching enzyme ofHendersonula toruloidea.},
  author={F J Odibo and Nduka Okafor and Moshe Tom and Christie A. Oyeka},
  journal={World journal of microbiology & biotechnology},
  year={1992},
  volume={8 2},
  pages={102-5}
}
An extracellular, debranching isoamylase fromHendersonula toruloidea ATCC 64930, grown on starch, was purified 12-fold to an electrophoretically homogeneous state. The purified enzyme (estimated mol wt 83000) was optimally active at pH 6.0 and 50°C and remained active when held at 70°C (30 min) and at pH 6 to 8 for 24 h. Na(+), Fe(2+) and Ba(2+) (at 5MM) enhanced enzyme activity while Hg(2+), Zn(2+) and Cu(2+) (at 5MM) were inhibitory. The enzyme hydrolysed amylopectin (Km, 0.25 mg/ml), forming… CONTINUE READING

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