Isolation, purification and functional characterization of Serine protease from a biocontrol agent Trichoderma harzianum

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Research Paper 01/07/2016
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Isolation, purification and functional characterization of Serine protease from a biocontrol agent Trichoderma harzianum

Muhammad Majid, Faiz Ahmad Joyia, Ghulam Mustafa, Muhammad Anjum Zia, Ghazala, Muhammad Sarwar Khan
Int. J. Biosci.9( 1), 376-383, July 2016.
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Abstract

Trichoderma harzianum is widely used as a biocontrol agent by virtue of its mycoparasitic abilities. An array of enzymatic proteins causing proteolysis of fungal cell wall make it competent parasite of numerous plant pathogenic fungi, protease is one such enzyme. In the present study Trichoderma harzianum producing extracellular protease was isolated from soil samples. The extracellular protease secreted by that Trichoderma isolate was purified to 41.13-fold and specific activity of the enzyme was calculated to be 145.42 U/mg. The purified enzyme was characterized for various optima. The study revealed higher stability levels of protease exhibiting upto 43% activity after an incubation of 30 min at 45°C and pH 10.0. The enzyme was found stable and highly active exclusively at strong alkaline conditions (pH=10) which showed its stability and suitability for various commercial applications. Moreover, the stability of enzyme illustrated its promising role in proficient mycoparastisic ability of Trichoderma isolate which can be employed as a biocontrol agent.

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