Extracellular pH 2.5 Optimum Acid Phosphatase fromAspergillus Ficuum: Immobilization On Modified Fractogel
- 1 December 1988
- journal article
- research article
- Published by Taylor & Francis in Preparative Biochemistry
- Vol. 18 (4) , 473-481
- https://doi.org/10.1080/00327488808062545
Abstract
Aspergillus ficuum pH 2.5 optimum acid phosphatase (orthophosphoric monoesters phosphohydrolase, E. C. 3.1.3.2) was covalently immbolized on 2-fluoro-1-methylpyridinium toluene-4-sulfonate (FMP)-activated Fractogel TSK HW-50F. The catalytic parameters and stability of the immobilized enzyme were compared with those of the free enzyme. While the Km and the temperature optima were unchanged, the K1 for orthophosphate was changed from 185 μM to 422 μM and greater stability was observed against heat treatment.This publication has 14 references indexed in Scilit:
- Purification, N-Terminal Amino Acid Sequence and Characterization of pH 2. 5 Optimum Acid Phosphatase (E.C. 3.1.3.2) from Aspergillus FicuumPreparative Biochemistry, 1987
- Extracellular Phytase (E. C. 3.1.3.8) fromAspergillus FicuumNRRL 3135: Purification and CharacterizationPreparative Biochemistry, 1987
- Structural genes for phosphatases inAspergillus nidulansGenetics Research, 1986
- Isolation and characterization of the structural gene for secreted acid phosphatase from Schizosaccharomyces pombe.Journal of Biological Chemistry, 1986
- A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250Analytical Biochemistry, 1977
- Purification and properties of one component of acid phosphatase produced by Aspergillus nigerBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Acid phosphatase of Aspergillus saitoi purification and properties.Agricultural and Biological Chemistry, 1977
- Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of the Partially Purified Phosphatases of Aspergillus ficuum NRRL 3135Australian Journal of Biological Sciences, 1974
- 19 Acid PhosphatasesPublished by Elsevier ,1971
- A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphataseBiochimica et Biophysica Acta, 1960