Current Progresses in Phytase Research: Three‐Dimensional Structure and Protein Engineering

Abstract

Phytase is one of the most important feed additive enzymes for monogastric animal, because it hydrolyzes the indigestible phytate in the cereal-based feedstock to release phosphate as an essential nutrient. To understand its molecular machinery, the three-dimensional structures of various types of phytases and complexes have been studied extensively. For commercial applications, important properties such as higher catalytic efficiency and higher thermostability are desired. Since a phytase with both beneficial characteristics is hardly found in nature, various protein engineering strategies are popular in modifying the existing enzymes with enhanced performance. In this review, the up-todate status of phytase structural and engineering studies is summarized. In addition, structural perspectives of some engineered phytases with improved properties are also provided. These results broaden the understanding of phytases and will be important for phytase applications in the future.

Microbial degradation of myo-inositol hexakisphosphate (IP6): specificity, kinetics, and simulation

“…Microbial phytases are of interest due to high substrate specificity, thermostability, catalytic efficiency, phosphate hydrolysis and low production cost (Chen et al 2015). The structure information of the enzyme is vital for its functional role.…”

New Bacterial Phytase through Metagenomic Prospection

“…β-Propeller phytases, also known as alkaline phytases, have been considered mainly identified in Bacillus species. More recent bioinformatics studies conducted on microbial genomes and environmental metagenomes suggested that the β-propeller phytases are distributed more widely than previously believed and may play a role in phytate–phosphorus cycling in soil and aquatic environment [ 25 ].…”

Globoids and Phytase: The Mineral Storage and Release System in Seeds

“…Briefly, HAPs fold into two domains: the α, and the larger α/β domain. The active site is made up of the conserved RHGXRXP and HD motifs, where the histidine of the first motive and the aspartate of the HD motif take direct part in the catalytic reaction [ 64 ]. Purple acid phosphatases are metalloproteins which contain a dinuclear Fe 3+ Me 2+ center in the active site.…”