| Title |
Production, Partial Characterization, and Immobilization in Alginate Beads of an Alkaline Protease from a New Thermophilic Fungus Myceliophthora sp. |
| Author |
Letícia Maria Zanphorlin1, Fernanda Dell Antonio Facchini2, Filipe Vasconcelos1, Rafaella Costa Bonugli-Santos3, André Rodrigues4, Lara Durães Sette3, Eleni Gomes1, and Gustavo Orlando Bonilla-Rodriguez1* |
| Address |
1UNESP - Univ Estadual Paulista IBILCE, São José do Rio Preto SP, 15054-000, Brazil, 2USP-University of São Paulo, Ribeirão Preto SP, 14049-900, Brazil, 3UNICAMP-State University of Campinas, CPQBA, Division of Microbial Resources, Campinas SP, 13081-970, Brazil, 4UNESP-Univ Estadual Paulista, Center for the Study of Social Insects, Rio Claro SP, 13506-900, Brazil |
| Bibliography |
Journal of Microbiology, 48(3),331-336, 2010,
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| DOI |
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| Key Words |
alkaline protease, immobilized enzyme, Myceliophthora sp., solid state fermentation, thermophilic fungus |
| Abstract |
Thermophilic fungi produce thermostable enzymes which have a number of applications, mainly in biotechnological processes. In this work, we describe the characterization of a protease produced in solidstate (SSF) and submerged (SmF) fermentations by a newly isolated thermophilic fungus identified as a putative new species in the genus Myceliophthora. Enzyme-production rate was evaluated for both fermentation processes, and in SSF, using a medium composed of a mixture of wheat bran and casein, the proteolytic output was 4.5-fold larger than that obtained in SmF. Additionally, the peak of proteolytic activity was obtained after 3 days for SSF whereas for SmF it was after 4 days. The crude enzyme obtained by both
SSF and SmF displayed similar optimum temperature at 50°C, but the optimum pH shifted from 7 (SmF) to 9 (SSF). The alkaline protease produced through solid-state fermentation (SSF), was immobilized on beads of calcium alginate, allowing comparative analyses of free and immobilized proteases to be carried out. It was
observed that both optimum temperature and thermal stability of the immobilized enzyme were higher than for the free enzyme. Moreover, the immobilized enzyme showed considerable stability for up to 7 reuses. |
