The purification and characterization of a Trichoderma harzianum exochitinase.

@article{Deane1998ThePA,
  title={The purification and characterization of a Trichoderma harzianum exochitinase.},
  author={E E Deane and John M. Whipps and Joseph M. Lynch and John F. Peberdy},
  journal={Biochimica et biophysica acta},
  year={1998},
  volume={1383 1},
  pages={101-10}
}
A chitinolytic enzyme was purified from the culture filtrate of T. harzianum (T198) by precipitation with ammonium sulphate followed by affinity binding to swollen chitin and release with 10% (v/v) acetic acid. The molecular weight of the enzyme was calculated to be 28 and 27.5 kD by gel filtration chromatography and SDS-PAGE, respectively. The isoelectric point of the enzyme was 7.4. The pH optimum for activity was 3.5 and maximum activity was obtained at 50 degrees C. The enzyme displayed… CONTINUE READING

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