The stability of Phytase activity from Burkholderia sp. strain HF.7

Phytase is an enzyme that hydrolyzes phytic acid but is not produced in the monogastricgastrointestinal tract of poultry. This study aims to discover the stability of extracellular phytaseBurkholderia sp. strain HF.7 under a range of temperature, pH, and protease activity conditionsincluding those similar to the digestive tract of poultry. Material and Methods: Temperature and pHstability tests were carried out at various temperatures (20-65 °C) and pH (1-8) by incubating thephytase in a Na-acetate buffer. The stability of phytase protease was further tested by adding thefollowing levels of proteases (pepsin and/or trypsin): P0: without protease, P1: pepsin (5000units/mL), P2: trypsin (5000 units/mL) and P3: pepsin + trypsin (2500 units/mL for each). ANOVAwas used to analyze the protease stability experiments (α=0.05). Finding: The results showed thatB. sp. strain HF.7 phytase had an optimum activity at 37 °C and pH 4; similar to the condition of thepoultry digestive tract in general. Conclusion: These findings suggest that B. sp. strain HF.7 haspotential to be used in poultry feed to increase productivity.