RT info:eu-repo/semantics/article
T1 Alkaline Phosphatase−Polyresorcinol Complex: Characterization and Application to Seed Coating
A1 Pilar Izquierdo, María Concepción
A1 Ortega Santamaría, Natividad
A1 Pérez Mateos, Manuel
A1 Busto Núñez, Mª Dolores
K1 Alkaline phosphatise
K1 Enzyme immobilization
K1 Enzyme−resorcinol complex
K1 Escherichia coli
K1 Hollow-bead
K1 Seed coating
K1 Bioquímica
K1 Biochemistry
K1 Biología molecular
K1 Molecular biology
AB An alkaline phosphatase (EC 3.1.3.1) from Escherichia coli ATCC27257 was immobilized by copolymerization with resorcinol. The phosphatase−polyresorcinol complex synthesized retained about 74% of the original enzymatic activity. The pH and temperature profile of the immobilized and free enzyme revealed a similar behavior. Kinetic parameters were determined: Km and Ki values were 2.44 and 0.423 mM, respectively, for the phosphatase−polyresorcinol complex and 1.07 and 0.069 mM, respectively, for free phosphatase. The thermal and storage stabilities of the immobilized phosphatase were higher than those of the native one. On addition to soil, free enzyme was completely inactivated in 4 days, whereas the phosphatase−polyresorcinol complex was comparatively stable. Barley seed coated with the immobilized enzyme exhibited higher rhizosphere phosphatase activity. Under pot culture conditions, an increase in the soil inorganic phosphorus was detected when the seed was encapsulated with the phosphatase−polyresorcinol complex, and a positive influence on biomass and inorganic phosphorus concentration of shoot was observed.
PB American Chemical Society
SN 0021-8561
YR 2009
FD 2009-03
LK http://hdl.handle.net/10259/8229
UL http://hdl.handle.net/10259/8229
LA eng
DS Repositorio Institucional de la Universidad de Burgos
RD 09-may-2024