PRODUCTION AND STABILITY OF LIPASE AND PECTINASE PRESENT IN AGROINDUSTRIAL RESIDUES

• Palavras-chave: Atena

• Keywords: enzymes; stability; agroindustrial residue.

• Abstract:

  Nowadays the reuse of agroindustrial

  residual has been outstanding in the scientific

  scenario by the aggregation of value and by the

  reduction of damages to the environment. Part

  of this residue are seeds of fruits and vegetables

  that usually have as final destination manure

  or animal feed. Among these residues are the

  seeds of mangaba, pumpkin, avocado and bark

  of avocado. The production of enzymes such

  as lipase and pectinase have been studied

  being extracted directly or using these residues

  as a substrate for fermentative processes.

  The objective of this study was to evaluate

  the presence of these enzymes in natural

  residues as well as their stability. The residues

  were triturated and buffer was added for the

  extracts to be produced. The extracts obtained

  were subjected to lipase and pectinase activity

  analyzes and the enzyme stabilities were

  checked after 2 hours at room temperature. The

  residues with the highest lipase activity were

  avocado seed and mangaba seed respectively

  (9.05 and 8.69 U / ml). The pumpkin seed also

  had an activity value close to the previous ones

  about 5.05 U / ml, whereas the avocado peel

  the activity of the lipase obtained was 1.43 U

  / ml much lower than the activities present in

  the seeds studied , thus showing that, for these

  residues, the enzyme concentration is higher

  in the seed than in the shell. For the pectinase

  activity the values obtained were closer

  between the residues studied and the highest

  was about 0.056 U / ml for the pumpkin seed.

  The enzymatic extracts analyzed showed a

  stability of about 50% within the time studied.

  We conclude, however, that these residues in

  natural, having presented enzymatic activity,

  can be used for future studies in the production

  of enzymes such as lipase and pectinase being

  an alternative for the use of the same.

• Número de páginas: 15