Evaluation of in vitro hydrolytic profile and anti-proteolytic activity of phytase produced by Aspergillus niger in poultry and pork rations

Abstract

Phytic acid is the largest form of phosphorus storage in plant seeds and is present as a large part of the organic phosphorus found in soil. However, phytate cannot be directly used by plants and some non-ruminant animals, such as pigs, birds and fish. Phytases form a class of phosphatase enzymes that have the activity of hydrolyzing phytate and releasing the orthophosphate ions bound to phytate estrus. Aqueous two-phase system is a method of extraction and purification, which is being considered an effective alternative in reducing steps of the purification processes. The objective of this work was to analyze the effect of pre-purified enzyme extract and post-purified extract on PEG / citrate SDFA on hydrolysis of phytic acid in commercial poultry and pork feeds, as well as to study the anti-proteolytic activity of the enzyme action of pepsin and trypsin. It is observed that the pre-purified enzyme was inhibited at phosphorus concentrations of 6 μmol of PO4-2, however the phytase after purified in PEG / citrate SDFA was inhibited at a lower phosphorus concentration than the pre-purified one. The enzymatic treatment of commercial poultry and pork rations using phytase from A. niger var. phoenicis URM 4924 was very promising, as it proved to be efficient in the phytate hydrolysis, releasing approximately 6 μmol of PO4-2, however with 4 U / mL of enzyme in 8 minutes of incubation. Phytase produced by A. niger var. phoenicis URM 4924 showed good performance in proteolytic resistance, as well as in phytate hydrolysis in commercial poultry and pork feeds, essential biochemical characteristics for an enzyme with potential industrial application.