Production,partial characterization,and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus <Emphasis Type="Italic">Myceliophthora</Emphasis> sp. |
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Authors: | Letícia Maria Zanphorlin Fernanda Dell Antonio Facchini Filipe Vasconcelos Rafaella Costa Bonugli-Santos André Rodrigues Lara Durães Sette Eleni Gomes Gustavo Orlando Bonilla-Rodriguez |
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Institution: | 1.UNESP - Univ Estadual Paulista IBILCE,S?o José do Rio Preto SP,Brazil;2.USP-University of S?o Paulo,Ribeir?o Preto SP,Brazil;3.Division of Microbial Resources,UNICAMP-State University of Campinas, CPQBA,Campinas SP,Brazil;4.Center for the Study of Social Insects,UNESP-Univ Estadual Paulista,Rio Claro SP,Brazil |
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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. |
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