STABILITY OF PECTINASE OF ASPERGILLUS NIGER IOC 4003 IN DIFFERENT SALTS FOR PURIFICATION IN BIPHASIC AQUEOUS SYSTEM.

• Palavras-chave: Atena

• Keywords: Pectinase, enzymatic stability, submerged fermentation, biphasic aqueous system.

• Abstract:

  Enzymes are commonly used in

  the food industry, paper, textiles, antifungals,

  among others. In purification processes of

  various substances such as enzymes of

  biotechnological origin, aqueous two-phase

  systems are widely used. Therefore, the aim

  of the study was to investigate the stability of

  pectinase in different salts for the definition

  of a biphasic aqueous system to be used

  in the purification of the enzyme. Pectinase

  was produced by submerged fermentation of

  Aspergillus Niger IOC 4003 using the mangaba

  depulped residue as the inducer. From stock

  solutions, extracts were conditioned for 2 h in the

  presence of 5, 10, 15 and 20% (m / m) of ethanol,

  ammonium sulfate, dibasic sodium phosphate

  and sodium citrate. Control assays were

   

  performed in the absence of these components

  with replacement by deionized water. In relation

  to the impact of the salts studied, the presence

  of the citrate and phosphate salts allowed

  greater stability in all the percentages used, with

  a dro in activity around 50%. In the presence

  of 10% ethanol, the relative activity was 422.81,

  being higher than that obtained with Citrate and

  Phosphate respectively 103.40 and 73.42 in

  the same percentage. For Sulfate, all relative

  activities obtained in the percentages studied

  were smaller than in the other trials. Thus, we

  consider that the stability of pectinase in the

  salts studied may aid in the selection of suitable

  phase-forming agents for the partitioning of this

  enzyme and its purification.

• Número de páginas: 15