Effect of Proteolytic Enzymes on Phytase Produced by Pseudomonas spp. Isolated from Local Chicken Faeces

Bulama Burah1*, Fatima Buba1, Yahaya Tijani1, Maina Isa Muhammad1, Abubakar Shettima2,
Babagana Modu1, Ali Abdullahi Damasak1, Abba Mohammed3, Rabiu Shehu Sa’ad1 and Mohammed Adamu Milala1

1Department of Biochemistry, Faculty of Life Sciences, University of Maiduguri, Nigeria.
2Department of Microbiology, Faculty of Life Sciences, University of Maiduguri, Nigeria.
3Department of Biochemistry, Yobe State University, Damaturu, Nigeria.

*Corresponding author’s Email: bulama19@gmail.com, doi.org/10.55639/607.02010099


ABSTRACT

Phytases are special types of phosphatases that catalyze the sequential hydrolysis of phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. Phytic acid is one of the main storage forms of phosphorus in plants. This study is aimed at investigating the effect of proteolytic enzymes on phytase activity. Standard methods were used during the investigations. The effects of proteolytic enzymes and gastric acid on crude phytase enzyme were studied. Phytase enzyme kinetics (KM and Vmax) were also determined using varying substrate concentrations. The results revealed that optimum phytase activity (0.53 µmol/min) was obtained when the crude phytase enzyme was treated with trypsin at 6.0% (v/v) while treatment with pepsin yielded highest activity (1.07 µmol/min) at 6.0% (v/v). A lower phytase activity was observed upon treatment with gastric acid. The double reciprocal graph of substrate concentration revealed that the KM and Vmax of phytase were 0.0029 mM and 3.744 µmol/min respectively. It could be concluded that the study demonstrated that crude phytase from Pseudomonas spp. retained measurable activity in the presence of proteolytic enzymes. These findings suggest potential suitability of the enzyme for application in animal nutrition.

KEYWORDS

Phytase,
Proteolytic
enzymes,
Pseudomonas spp,
Phytic acid.

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