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World J Microbiol Biotechnol ; 30(6): 1755-62, 2014 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-24419660

RESUMO

Endophytes are recognised as potential sources of novel secondary metabolites, including enzymes and drugs, with applications in medicine, agriculture and industry. There is a growing need for new enzymes, including proteases, for use in industry that can function under a variety of conditions. In this study, three fungal endophytes (Alternaria alternata, Phoma herbarum and an unclassified fungus), were isolated from the Australian native plant, Eremophilia longifolia, and assessed for production of proteases. The lyophilised growth media obtained after fungal fermentation were analysed for protease production using enzyme activity assays. Protease production was optimised by assessing the effects of temperature, pH, carbon source and nitrogen source on activity. A. alternata showed the greatest protease activity in a wide range of pH (3-9). The broadest activity between 9 and 50 °C was observed at pH 7, suggesting a neutral protease. Overall, the optimum conditions were 37 °C and pH 7 with a maximum specific activity value of 69.86 BAEE units/mg. The characteristics demonstrated by this fungal endophyte showed that it is a potential source of an enzyme with particular application in the dairy industry. However, further studies of the tolerance to higher temperatures and pH will indicate whether the enzyme is suitable to such applications.


Assuntos
Alternaria/enzimologia , Endófitos/enzimologia , Eremophila (Planta)/microbiologia , Proteínas Fúngicas/metabolismo , Peptídeo Hidrolases/metabolismo , Alternaria/química , Alternaria/genética , Alternaria/isolamento & purificação , Austrália , Meios de Cultura/química , Meios de Cultura/metabolismo , Endófitos/química , Endófitos/genética , Endófitos/isolamento & purificação , Estabilidade Enzimática , Fermentação , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Temperatura Alta , Concentração de Íons de Hidrogênio , Peptídeo Hidrolases/química , Peptídeo Hidrolases/genética
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