Purification and Properties of Catalase from Van Apple (Golden Delicious)

Authors

  • I.H. Yoruk Department of Chemistry, Art and Science Faculty, University of Yuzunco Yil, Van, Türkiye
  • H. Demir Department of Chemistry, Art and Science Faculty, University of Yuzunco Yil, Van, Turkey
  • K. Ekici Department of Food Hygiene and Technology, Veterinary College, University of Yuzunco Yil, Van, Türkiye
  • A. Savran Department of Chemistry, Art and Science Faculty, University of Yuzunco Yil, Van, Turkey

DOI:

https://doi.org/10.3923/pjn.2005.8.10

Keywords:

Catalase, characterization, purification, inhibitors

Abstract

Catalase (CAT:EC1.11.1.6) was purified from Van Apple. The purified enzyme preparation was obtained with a final recovery of enzyme activity of about 11.5% and a specific activity of 29.43 U/mg proteins. The purified catalase has an optimum temperature of activity at 50oC. As regards pH, the enzyme has an optimum activity of pH 5. Vmax and Km values were determined by Lineweaver-burk graphs. Potassium cyanide, citric acid, MnCl2, NaCl, NaNO2 and CuSO4 were used as inhibitor.

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Published

15.12.2004

Issue

Vol. 4 No. 1 (2005)

Section

Research Article

License

Copyright (c) 2005 Asian Network for Scientific Information

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited.

How to Cite

1.
Yoruk I, Demir H, Ekici K, Savran A. Purification and Properties of Catalase from Van Apple (Golden Delicious). Pak. J. Nutr. [Internet]. 2004 Dec. 15 [cited 2025 Jul. 1];4(1):8-10. Available from: https://pjnonline.org/pjn/article/view/207

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