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Pakistan Journal of Biological Sciences

Year: 2001 | Volume: 4 | Issue: 3 | Page No.: 271-276
DOI: 10.3923/pjbs.2001.271.276

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Authors


Jwanny E. W.

Country: Egypt

S. T. El-Sayed

Country: Egypt

A. M. Salem

Country: Egypt

A. N. Shehata

Country: Egypt

Keywords


  • Chitinase
  • laminarinase
  • aspergillus species
  • antifungal
  • activity
Research Article

Characterization and Antifungal Evaluation of Chitinase and Laminarinases from Sugar Beet Leaves

Jwanny E. W., S. T. El-Sayed, A. M. Salem and A. N. Shehata
Chitinase, laminarinase A and laminarinase B were extracted and purified from Egyptian sugar beet (Beta vulgaris) leaves. Chitinase showed higher heat stability than laminarinase A and laminarinase B when heated at 50°C for 60 min. Chitinase activity was quite stable in water than in buffer, while laminarinase A and laminarinase B activities increased when incubated with 0.1M citrate-phosphate buffer at pH 6.0 to 7.0 for 30 min. The Km values of chitinase, laminarinase A and laminarinase B were 0.2, 0.27 and 0.074% at pH`s 4.5, 4.5 and 6.5 using colloidal chitin, laminarin A and laminarin B as substrates respectively. Chitinase enzyme was activated by 0.75 mM - mercaptoethanol by 1.6 times, while laminarinase A enzyme was activated by 1.0 mM of CuCl2, FeSO4 and EDTA with 2.35, 1.38 and 1.57 times respectively. Laminarinase B enzyme was activated by 1.0 mM Zn SO4 and K2SO4 with 1.3 and 1.18 times respectively. Chitinase, laminarinase A and laminarinase B enzymes have an endo-splitting type of activity. They were able to inhibit the growth and to lyse cell walls of Aspergillus oryza and A. flavus either alone or in combination through the degradation of chitin and laminarin.

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How to cite this article

Jwanny E. W., S. T. El-Sayed, A. M. Salem and A. N. Shehata, 2001. Characterization and Antifungal Evaluation of Chitinase and Laminarinases from Sugar Beet Leaves. Pakistan Journal of Biological Sciences, 4: 271-276.

DOI: 10.3923/pjbs.2001.271.276

URL: https://scialert.net/abstract/?doi=pjbs.2001.271.276

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