Purification and biochemical characterization of a mycelial alkaline phosphatase without DNAase activity produced byAspergillus caespitosus
Biochemical properties of a termostable alkaline phosphatase obtained from the mycelium extract ofA. caespitosus were described. The enzyme was purified 42-fold with 32 % recovery by DEAE-cellulose and concanavalin A-Sepharose chromatography. The molar mass estimated by Sephacryl S-200 or by 7 % SDS...
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| Published in | Folia microbiologica Vol. 52; no. 3; pp. 231 - 236 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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Dordrecht
Springer Nature B.V
01.05.2007
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| Abstract | Biochemical properties of a termostable alkaline phosphatase obtained from the mycelium extract ofA. caespitosus were described. The enzyme was purified 42-fold with 32 % recovery by DEAE-cellulose and concanavalin A-Sepharose chromatography. The molar mass estimated by Sephacryl S-200 or by 7 % SDS-PAGE was 138 kDa and 71 kDa, respectively, indicating a homodimer. Temperature and pH optima were 80 °C and pH 9.0. This enzyme was highly glycosylated (≈74 % saccharide content). The activity was enhanced by Mg2+ (19–139 %), NH4+ (64 %), Na+ (51 %) and Mn2+ (38 %). 4-Nitrophenyl phosphate (4-NPP) was preferentially hydrolyzed, but glucose 1-phosphate (93 %), UTP (67 %) andO-phosphoamino acids also acted as substrates.νlim andKm were 3.78 nkat per mg protein and 270 µmol/L in the absence of Mg2+ and 7.35 nkat per mg protein and 410 µmol/L in the presence of Mg2+, using 4-NPP as substrate. The purified alkaline phosphatase removed the 5′-phosphate group of a linearized plasmid without showing DNAase activity, indicating its potential for recombinant DNA technology. |
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| AbstractList | Biochemical properties of a termostable alkaline phosphatase obtained from the mycelium extract ofA. caespitosus were described. The enzyme was purified 42-fold with 32 % recovery by DEAE-cellulose and concanavalin A-Sepharose chromatography. The molar mass estimated by Sephacryl S-200 or by 7 % SDS-PAGE was 138 kDa and 71 kDa, respectively, indicating a homodimer. Temperature and pH optima were 80 °C and pH 9.0. This enzyme was highly glycosylated (≈74 % saccharide content). The activity was enhanced by Mg2+ (19–139 %), NH4+ (64 %), Na+ (51 %) and Mn2+ (38 %). 4-Nitrophenyl phosphate (4-NPP) was preferentially hydrolyzed, but glucose 1-phosphate (93 %), UTP (67 %) andO-phosphoamino acids also acted as substrates.νlim andKm were 3.78 nkat per mg protein and 270 µmol/L in the absence of Mg2+ and 7.35 nkat per mg protein and 410 µmol/L in the presence of Mg2+, using 4-NPP as substrate. The purified alkaline phosphatase removed the 5′-phosphate group of a linearized plasmid without showing DNAase activity, indicating its potential for recombinant DNA technology. Biochemical properties of a termostable alkaline phosphatase obtained from the mycelium extract ofA. caespitosus were described. The enzyme was purified 42-fold with 32 % recovery by DEAE-cellulose and concanavalin A-Sepharose chromatography. The molar mass estimated by Sephacryl S-200 or by 7 % SDS-PAGE was 138 kDa and 71 kDa, respectively, indicating a homodimer. Temperature and pH optima were 80 C and pH 9.0. This enzyme was highly glycosylated (-74 % saccharide content). The activity was enhanced by Mg super(2+) (19-139 %), NH sub(4) super(+) (64 %), Na super(+) (51 %) and Mn super(2+) (38 %). 4-Nitrophenyl phosphate (4-NPP) was preferentially hydrolyzed, but glucose 1-phosphate (93 %), UTP (67 %) andO-phosphoamino acids also acted as substrates. sub(lim) andK sub(m) were 3.78 nkat per mg protein and 270 kmol/L in the absence of Mg super(2+) and 7.35 nkat per mg protein and 410 kmol/L in the presence of Mg super(2+), using 4-NPP as substrate. The purified alkaline phosphatase removed the 5'-phosphate group of a linearized plasmid without showing DNAase activity, indicating its potential for recombinant DNA technology. |
| ArticleNumber | 231 |
| Author | Guimarães, L. H. S. Terenzi, H. F. Polizeli, M. L. T. M. Júnior, A. B. Jorge, J. A. |
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| SubjectTerms | Alkaline phosphatase Biochemistry Carbohydrates Cellulose Concanavalin A Deoxyribonucleic acid DNA Enzymes Gel electrophoresis Magnesium Microbiology Mycelia pH effects Proteins Recombinant DNA Sodium lauryl sulfate Substrates |
| Title | Purification and biochemical characterization of a mycelial alkaline phosphatase without DNAase activity produced byAspergillus caespitosus |
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