Bioprocess for efficient production of recombinant Pichia anomala phytase and its applicability in dephytinizing chick feed and whole wheat flat Indian breads

Abstract

The phytase of the yeast Pichia anomala (PPHY) is a suitable biocatalyst as a food and feed additive because of its adequate thermostability, acid stability, protease insensitivity and broad substrate spectrum. The cell-bound nature and low phytase titres are the main bottlenecks for its utility in food and feed industries. In this investigation, we have overcome the problems by constitutive secretory expression of PPHY under glyceraldehyde phosphate dehydrogenase (GAP) promoter. A ~44-fold increase in rPPHY titre has been achieved after optimization of cultural variables by one-variable-at-a-time approach and two factorial statistical design. The use of GAP promoter makes the cultivation of the recombinant P. pastoris straight forward and eliminates the requirement of methanol for induction and hazards associated with its storage. Among metal-phytate complexes, Ca(2+) phytate is hydrolyzed more efficiently by rPPHY than Co(2+), Mn(2+), Mg(2+), Fe(3+) and Zn(2+) phytates. The enzyme is effective in dephytinizing whole wheat unleavened flat Indian breads (naan and tandoori) and different broiler feeds, thus mitigating anti-nutritional effects of phytates.

Production, characterization, and applications of a novel thermo-acidophilic L-asparaginase of Pseudomonas aeruginosa CSPS4

“…Very similar parameters were reported to produce L-asparaginase from another P. aeruginosa strain, where 1% (w/v) asparagine and glucose were reported for the maximum productivity after 48 hrs incubation at 35 °C (Amany et al 2021). Statistical optimization using PB and Response Surface Methodology (RSM) is always beneficial to understand the interaction among the physical and chemical parameters for enhancing the production of enzymes (Sharma and Satyanarayana 2011;Joshi and Satyanarayana 2015;Talluri et al 2019). Here, the results of this study observed maximum Lasparaginase production from 19.55±2.77 nM/min (4 th run) to 521.33±4.07 nM/min units (10 th run) during the PB analysis.…”