Isolation and biochemical characterization of phytase from different sources
International Journal of Development Research
Isolation and biochemical characterization of phytase from different sources
Received 04th December, 2016; Received in revised form 19th January, 2017; Accepted 27th February, 2017; Published online 31st March, 2017
Copyright©2017, Chaitanya Mogal et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Phytase (myo-inositolhexakisphosphate phosphohydrolase) catalyzes the hydrolysis of myo-inositol hexakisphosphate (phytic acid) to inorganic monophosphate and lower myo-inositol phosphates, and in some cases to free myo-inositol. Two bacterial strains, one fungal strain and one plant source were screened for phytate degradation viz. Escherichia coli (ATCC 25922), Bacillus subtilis (ATCC 6633), Aspergillus niger (ATCC 16888) and Glycine max (JS-335). Among these, B. subtilis (ATCC 6633) strain was found to produce maximum clearance zone of 2.7 cm on phytase screening medium containing sodium phytate as substrate, incubated at 37 °C for 48 hours. Phytase was isolated from B. subtilis (ATCC 6633), which was able to withstand temperature ranging from 40 °C to 50 °C, pH 4.0- 6.0 and showed maximum activity at 50 °C and 6.0 pH. However, phytase isolated from E.coli (ATCC 25922), A.niger (ATCC 16888) and Glycine max (JS-335) were able to withstand temperature ranging from 37.5 °C to 45 °C only and at pH 3.5-5.0.
