Production and action of an Aspergillus phoenicis enzymatic pool using different carbon sources

• Autor(a) principal: Benassi,Vivian Machado
• Data de Publicação: 2012
• Outros Autores: Lucas,Rosymar Coutinho de, Michelin,Michele, Jorge,João Atílio, Terenzi,Héctor Francisco, Polizeli,Maria de Lourdes Teixeira de Moraes
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Food Technology
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1981-67232012000300009
• topic: Aspergillus phoenicis; Amylase; Rye flakes; Potato starch; Cassava flour

Aspergillus phoenicis is an interesting heat tolerant fungus that can synthesize enzymes with several applications in the food industry due to its great hydrolytic potential. In this work, the fungus produced high enzymatic levels when cultivated on inexpensive culture media consisting of flakes from different origins such as cassava flour, wheat fibre, crushed soybean, agro-industrial wastes, starch, glucose or maltose. Several enzymatic systems were produced from these carbon sources, but amylase was the most evident, followed by pectinase and xylanase. Traces of CMCases, avicelase, lipase, β-xylosidase, β-glucosidase and α-glucosidase activities were also detected. Amylases were produced on rye flakes, starch, oat flakes, corn flakes, cassava flour and wheat fibre. Significant amylolytic levels were produced in the culture medium with glucose or when this sugar was exhausted, suggesting an enzyme in the constitutive form. Cassava flour, rye, oats, barley and corn flakes were also used as substrates in the hydrolytic reactions, aiming to verify the liberation potential of reducing sugars. Corn flakes induced greater liberation of reducing sugars as compared to the others. Thin layer chromatography of the reaction end products showed that the hydrolysis of cassava flour liberated maltooligosaccharides, but cassava flour and corn, rye, oats and barley flakes were hydrolyzed to glucose. These results suggested the presence of glucoamylase and α-amylase as part of the enzymatic pool of A. phoencis.