Characteristics and Applicability of Phytase of the Yeast Pichia anomala in Synthesizing Haloperoxidase

Abstract

The phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids identified by site-directed mutagenesis. Among modulators, N-bromosuccinimide and butanedione inhibit phytase, while Ca(2+) and Ni(2+) stimulate slightly. Vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with phytate. The T 1/2, activation energy (E a ), temperature quotient (Q 10), activation energy of thermal inactivation (Ed), and enthalpy (ΔH d (0) ) of the enzyme are 4.0 min (80 °C), 27.72 kJ mol(-1), 2.1, 410.62 kJ mol(-1), and ∼407.8 kJ mol(-1) (65-80 °C), respectively. The free energy of the process (ΔG d (o) ) increases from 49.56 to 71.58 kJ mol(-1) with rise in temperature, while entropy of inactivation (ΔS d (0) ) remains constant at ∼1.36 kJ mol(-1) K(-1). The supplementation of whole wheat dough with rPPHY resulted in 72.5 % reduction in phytic acid content of bread. These characteristics confirm that the phytase has adequate thermostability for its applicability as a food and feed additive.

Characteristics of Recombinant Phytase (rSt-Phy) of the Thermophilic mold Sporotrichum thermophile and its applicability in dephytinizing foods

“…Free energy change (ΔG) is positive for rSt-Phy, which indicates that the thermal denaturation of recombinant enzyme is non-spontaneous as reported for the recombinant phytase of P. anomala [43]. Denaturation of the enzyme is accompanied by the increase in the disorder of the enzyme structure which can be measured as entropy change (ΔS) which decreases with increasing enzyme stability.…”

Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications

“…This species exhibits antimicrobial activities and flavoring features that are responsible for its frequent association with food, beverages, and feed products [ 13 ]. Joshi and Satyanarayana [ 55 ] described phytase from P. anomala as a HAP that is thermostable and used as a feed additive. The PPHY gene of P. anomala synthesizes a cell-bound phytase with an ORF of 1389 bp encoding a 462-amino acid protein [ 53 ].…”

Biosynthesis, purification, kinetic and thermodynamic analysis of phytase from Aspergillus oryzae

“…The thermodynamic characteristic of an enzyme is the utilization of substrate by an enzyme with changing the temperature. The energy of activation (Ea), entropy (∆S) and enthalpy (∆H) are essential thermodynamic parameters, which are considered while analyzing the efficiency of an enzyme (Joshi and Satyanarayana, 2015).…”