4.0 Article

Bioprospection and characterization of the amylolytic activity by filamentous fungi from Brazilian Atlantic Forest

期刊

BIOTA NEOTROPICA
卷 17, 期 3, 页码 -

出版社

REVISTA BIOTA NEOTROPICA
DOI: 10.1590/1676-0611-BN-2017-0337

关键词

Amylase; Filamentous fungi; Aspergillus brasiliensis; Rhizopus oryzae; Glucoamylase; Bioprospection

资金

  1. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo ( FAPESP)
  2. Conselho de Desenvolvimento Cientifico e Tecnologico (CNPq)
  3. National System for Research on Biodiversity (Sisbiota- Brazil) [CNPq 563260/2010, 2010/52322-3]
  4. CNPq
  5. FAPESP [2013/01437-3]

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Filamentous fungi are widely diverse and ubiquitous organisms. Such biodiversity is barely known, making room for a great potential still to be discovered, especially in tropical environments - which are favorable to growth and species variety. Filamentous fungi are extensively applied to the production of industrial enzymes, such as the amylases. This class of enzymes acts in the hydrolysis of starch to glucose or maltooligosaccharides. In this work twenty-five filamentous fungi were isolated from samples of decomposing material collected in the Brazilian Atlantic Forest. The two best amylase producers were identified as Aspergillus brasiliensis and Rhizopus oryzae. Both are mesophilic, they grow well in organic nitrogen-rich media produce great amounts of glucoamylases. The enzymes of A. brasiliensis and R. oryzae are different, possibly because of their phylogenetical distance. The best amylase production of A. brasiliensis occurred during 120 hours with initial pH of 7.5; it had a better activity in the pH range of 3.5-5.0 and at 60-75 degrees C. Both fungal glucoamylase had wide pH stability (3-8) and were activated by Mn2+. R. oryzae best production occurred in 96 hours and at pH 6.5. Its amylases had a greater activity in the pH range of 4.0-5.5 and temperature at 50-65 degrees C. The most significant difference between the enzymes produced by both fungi is the resistance to thermal denaturation: A. brasiliensis glucoamylase had a T-50 of 60 minutes at 70 degrees C. The R. oryzae glucoamylase only had a residual activity when incubated at 50 degrees C with a 12 min T-50.

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