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 Ca2+ and Ni2+ 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 (E-d), and enthalpy (Delta H (d) (0) ) of the enzyme are 4.0 min (80 A degrees C), 27.72 kJ mol(-1), 2.1, 410.62 kJ mol(-1), and 407.8 kJ mol(-1) (65-80 A degrees C), respectively. The free energy of the process (Delta G (d) (o) ) increases from 49.56 to 71.58 kJ mol(-1) with rise in temperature, while entropy of inactivation (Delta S (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.