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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Commodity Utilization Research » Research » Publications at this Location » Publication #311707

Title: Phosphatase hydrolysis of organic phosphorus compounds

Author
item TAZISONG, IRENUS - Alabama A & M University
item SENWO, ZACHARY - Alabama A & M University
item He, Zhongqi

Submitted to: Advances in Enzyme Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/15/2015
Publication Date: 6/24/2015
Citation: Tazisong, I.A., Senwo, Z.N., He, Z. 2015. Phosphatase hydrolysis of organic phosphorus compounds. Advances in Enzyme Research. 3:39-51.

Interpretive Summary: Phosphatases are soil enzymes that deserve special attention because of the significant roles they play in mineralizing organic phosphorus (P) into inorganic available form. For getting more insight on the enzymatically hydrolysis of organic P, in this work, we compared the catalytic parameters of commercially available wheat germ, sweet potato, and potato acid phosphatase and alkaline phosphatase from E. coli. These four enzymes were selected because they have been used in characterization and quantification of organic P in animal manure, soil and other environmental samples. This study indicates that phosphatases exhibit a broad range of substrate specificity. The rate of hydrolysis, catalytic efficiency, thermal stability, and optimal pH of these enzymes may depend on enzyme sources and the stereochemical or stereoisomeric structures of the substrates. Knowledge derived from this work would be helpful in better understanding of enzyme activities in soils and water environments.

Technical Abstract: Phosphatases are diverse groups of enzymes that deserve special attention because of the significant roles they play in mineralizing organic phosphorus (P) into inorganic available form. For getting more insight on the enzymatically hydrolysis of organic P, in this work, we compared the catalytic parameters of commercially available wheat germ, sweet potato, and potato acid phosphatase and alkaline phosphatase from E. coli. This study demonstrated that the rate of hydrolysis, catalytic efficiency, thermal stability, and optimal pH of these enzymes depended on enzyme sources and the stereochemical or stereoisomeric structures of the substrates. This study also revealed that both acid and alkaline phosphatases exhibited broad ranges of substrate specificity with high affinity for P-nitrophenyl phosphate bis (cyclohexylammonium) than the commonly used P-nitrophenyl phosphate disodium hexahydrate. Sweet potato acid phosphatase had enhanced reaction kinetics with most tested substrates, compared to wheat germ and potato acid phosphatases. The optimum pH for the acid phosphatase was observed to be 5.0. Generally, the activity of alkaline phosphatase was similar to that of the acid phosphatase with optimal pH between 10-13, depending on the substrates. Knowledge derived from this work would be helpful in better understanding of enzyme activities in soils and water environments.