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Purification and Characterization of Alkaline Proteases from Aspergillus terreus

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dc.contributor.author AHSAN HUSSAIN
dc.contributor.author ABDUL MANNAN
dc.contributor.author HASSAN ZUBAIR
dc.contributor.author BUSHRA MIRZA
dc.date.accessioned 2023-11-07T07:42:32Z
dc.date.available 2023-11-07T07:42:32Z
dc.date.issued 2010-08-20
dc.identifier.citation Hussain, A., Manan, H., Zubair, H., & Mirza, B. (2010). Purification and characterization of alkaline proteases from Aspergillus terrus. J. Chem. Soc. Pak, 32(4), 497-504. en_US
dc.identifier.issn 0253-5106
dc.identifier.uri http://142.54.178.187:9060/xmlui/handle/123456789/19928
dc.description.abstract Proteases belong to an important class of enzymes known as hydrolases and catalyze hydrolysis of proteins. They act primarily to degrade proteins that are used for energy production and as biosynthetic precursors. In the following study, protease produced from Aspergillus terreus was found to be thermostable and included in the category of alkaline serine and metalloprotease. During partial purification, presence of enzyme in 60% (NH₄)₂SO₄ indicated small molecular weight polypeptide; later purification with Sephadex G-75 fractionation yielded a single proteolytic active molecule. At final purification step, the increase in specific activity of the enzyme was 7.5 fold with 23% yield. SDS-PAGE analysis revealed that alkaline protease of Aspergillus terreus is a monomer with approximate molecular weight of 35 kDa. Optimum pH for protease activity was found in the range of 7.5-11.0 (maximum at pH 8.5), thus apparently classified as an alkaline protease. The enzyme was thermostable towards high temperature (60 °C), however it denatured irreversibly at 70 °C showing 80% loss of activity. The maximum proteolytic activity was found at 40 °C. The enzyme was effectively inhibited by PMSF, EDTA and urea whereas iodoacetamide and thiourea did not result in any loss in activity while cysteine was found to be activator molecule. The study with metal ions Mg⁺², Mn⁺² and Fe⁺³ (1 mM each) showed minute stimulatory effects on enzyme activity. Co⁺² and Ca⁺² (1 mM) had neither excitatory nor inhibitory effect while Hg⁺² and Cu⁺² (1 mM) slightly reduced the enzyme activity. en_US
dc.description.sponsorship The chemical society of Pakistan is an approved society from the PSF. en_US
dc.language.iso en en_US
dc.publisher HEJ Research Institute of Chemistry, University of Karachi, Karachi. en_US
dc.title Purification and Characterization of Alkaline Proteases from Aspergillus terreus en_US
dc.type Article en_US


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