Fungal Alpha-Galactosidase from Pseudobalsamia microspora Capable of Degrading Raffinose Family Oligosaccharides
An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemica...
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| Vydáno v: | Applied biochemistry and biotechnology Ročník 176; číslo 8; s. 2157 - 2169 |
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| Médium: | Journal Article |
| Jazyk: | angličtina |
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Springer US
01.08.2015
Springer Nature B.V |
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| ISSN: | 0273-2289, 1559-0291, 1559-0291 |
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| Abstract | An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg²⁺, Cd²⁺, Cu²⁺, and Fe³⁺ ions. Three inner peptide sequences for PMG were obtained by liquid chromatography–tandem mass spectrometry (LC–MS–MS) analysis. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K ₘ) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V ₘₐₓ) was 0.97 μmol ml⁻¹ min⁻¹. Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. |
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| AbstractList | An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg(2+), Cd(2+), Cu(2+), and Fe(3+) ions. Three inner peptide sequences for PMG were obtained by liquid chromatography-tandem mass spectrometry (LC-MS-MS) analysis. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K m) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V max) was 0.97 μmol ml(-1) min(-1). Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries.An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg(2+), Cd(2+), Cu(2+), and Fe(3+) ions. Three inner peptide sequences for PMG were obtained by liquid chromatography-tandem mass spectrometry (LC-MS-MS) analysis. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K m) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V max) was 0.97 μmol ml(-1) min(-1). Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg(2+), Cd(2+), Cu(2+), and Fe(3+) ions. Three inner peptide sequences for PMG were obtained by liquid chromatography-tandem mass spectrometry (LC-MS-MS) analysis. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K m) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V max) was 0.97 μmol ml(-1) min(-1). Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg²⁺, Cd²⁺, Cu²⁺, and Fe³⁺ ions. Three inner peptide sequences for PMG were obtained by liquid chromatography–tandem mass spectrometry (LC–MS–MS) analysis. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K ₘ) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V ₘₐₓ) was 0.97 μmol ml⁻¹ min⁻¹. Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg²⁺, Cd²⁺, Cu²⁺, and Fe³⁺ ions. Three inner peptide sequences for PMG were obtained by liquid chromatography–tandem mass spectrometry (LC–MS–MS) analysis. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K ₘ) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V ₘₐₓ) was 0.97 μmol ml⁻¹ min⁻¹. Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg super(2+), Cd super(2+), Cu super(2+), and Fe super(3+) ions. Three inner peptide sequences for PMG were obtained by liquid chromatography-tandem mass spectrometry (LC-MS-MS) analysis. When 4-nitrophenyl alpha -d-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 degree C, respectively. The Michaelis constant (K sub(m)) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V sub(max)) was 0.97 mu mol ml super(-1) min super(-1). Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N -bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg 2+ , Cd 2+ , Cu 2+ , and Fe 3+ ions. Three inner peptide sequences for PMG were obtained by liquid chromatography–tandem mass spectrometry (LC–MS–MS) analysis. When 4-nitrophenyl α- d -glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant ( K m ) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity ( V max ) was 0.97 μmol ml −1 min −1 . Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62 kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg^sup 2+^, Cd^sup 2+^, Cu^sup 2+^, and Fe^sup 3+^ ions. Three inner peptide sequences for PMG were obtained by liquid chromatography-tandem mass spectrometry (LC-MS-MS) analysis. When 4-nitrophenyl [alpha]-d-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55 °C, respectively. The Michaelis constant (K ^sub m^) value of the alpha-galactosidase on pNPGal was 0.29 mM, and the maximal velocity (V ^sub max^) was 0.97 [mu]mol ml^sup -1^ min^sup -1^. Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries. |
| Author | Zhao, Yongchang Zhao, Liyan Wang, Hexiang Tian, Guoting Ng, Tzi Bun Yang, Dongxue Du, Fang |
| Author_xml | – sequence: 1 fullname: Yang, Dongxue – sequence: 2 fullname: Tian, Guoting – sequence: 3 fullname: Du, Fang – sequence: 4 fullname: Zhao, Yongchang – sequence: 5 fullname: Zhao, Liyan – sequence: 6 fullname: Wang, Hexiang – sequence: 7 fullname: Ng, Tzi Bun |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26184012$$D View this record in MEDLINE/PubMed |
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| Snippet | An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange... An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange... An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5 units/mg by ion-exchange... |
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| SubjectTerms | alpha-galactosidase alpha-Galactosidase - chemistry alpha-Galactosidase - isolation & purification alpha-Galactosidase - metabolism Amino Acid Sequence Amino acids Bacteria Biochemistry Biotechnology cadmium Chemistry Chemistry and Materials Science chromatography Chromatography, Ion Exchange Chromatography, Thin Layer copper Electrophoresis, Polyacrylamide Gel essential amino acids Feed industry Filtration Fungi gel chromatography Hydrogen-Ion Concentration Hydrolysis Indicators and Reagents ion exchange chromatography Ions iron Kinetics Liquid chromatography Mass spectrometry mercury Metals - pharmacology Microspora Microsporidia - enzymology Microsporidia - isolation & purification Molecular Sequence Data Molecular Weight Mushrooms polyacrylamide gel electrophoresis raffinose Raffinose - metabolism stachyose Substrate Specificity - drug effects tandem mass spectrometry Temperature Thin layer chromatography |
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| Title | Fungal Alpha-Galactosidase from Pseudobalsamia microspora Capable of Degrading Raffinose Family Oligosaccharides |
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