<b>Production and partial characterization of proteases from <i>Mucor hiemalis</i> URM3773

Acta Scientiarum : Biological Sciences. 2015;37(1):71-79 DOI 10.4025/actascibiolsci.v37i1.21016


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Journal Title: Acta Scientiarum : Biological Sciences

ISSN: 1679-9283 (Print); 1807-863X (Online)

Publisher: Eduem - Editora da Universidade Estadual de Maringá

LCC Subject Category: Science: Biology (General) | Science: Microbiology

Country of publisher: Brazil

Language of fulltext: English

Full-text formats available: PDF



Roana Cecília dos Santos Ribeiro (Universidade Federal Rural de Pernambuco)
Thaís Rafaelle dos Santos Ribeiro (Universidade Federal de Campina Grande)
Cristina Maria de Souza-Motta (Universidade Federal de Pernambuco)
Erika Valente Medeiros (Universidade Federal Rural de Pernambuco)
Keila Aparecida Moreira (Universidade Federal Rural de Pernambuco)


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Time From Submission to Publication: 38 weeks


Abstract | Full Text

The current study evaluated the proteases production from 11 fungal species belonging to the genera Mucor, Rhizomucor and Absidia. The species were obtained from the Collection of Cultures URM at the Mycology Department-UFPE, Brazil. The best producing species was Mucor hiemalis URM 3773 (1.689 U mL-1). Plackett-Burman design methodology was employed to select the most effective parameter for protease production out of 11 medium components, including: concentration of filtrate soybean, glucose, incubation period, yeast extract, tryptone, pH, aeration, rotation, NH4Cl, MgSO4 and K2HPO4. Filtrated soybean concentration was the significant variable over the response variable, which was the specific protease activity. The crude enzyme extract showed optimal activity in pH 7.5 and at 50ºC. The enzyme was stable within a wide pH range from 5.8 to 8.0, in the phosphate buffer 0.1M and in stable temperature variation of 40-70ºC, for 180 minutes. The ions FeSO4, NaCl, MnCl2, MgCl2 and KCl stimulated the protease activity, whereas ZnCl2 ion inhibited the activity in 2.27%. Iodoacetic acid at 1mM was the proteases inhibitor that presented greater action.The results indicate that the studied enzyme have great potential for industrial application.