Purification, characterization, and mode of action of a rhamnogalacturonan hydrolase from Irpex lacteus, tolerant to an acetylated substrate
A novel rhamnogalacturonase (RGase) acting on an acetylated substrate was detected in the commercial preparation Driselase, an enzymatic mixture derived from the basidiomycete Irpex lacteus. The activity was isolated by hydrophobic interaction chromatography, gel filtration, and preparative isoelect...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2010-03, Vol.86 (2), p.577-588 |
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| creator | Normand, Jessica Ralet, Marie-Christine Thibault, Jean-François Rogniaux, Hélène Delavault, Philippe Bonnin, Estelle |
| description | A novel rhamnogalacturonase (RGase) acting on an acetylated substrate was detected in the commercial preparation Driselase, an enzymatic mixture derived from the basidiomycete Irpex lacteus. The activity was isolated by hydrophobic interaction chromatography, gel filtration, and preparative isoelectric focusing, resulting in the isolation of five different rhamnogalacturonan hydrolases exhibiting various isoelectric points from 6.2 to 7.7. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and mass spectrometry analyses after trypsin cleavage of the five fractions revealed that the five rhamnogalacturonases have a molar mass of 55 kDa without any divergences in the identified peptides. The RGase with a pI of 7.2 exhibited a pH optimum between 4.5 and 5 and a temperature optimum between 40°C and 50°C. Its mode of action was analyzed by mass spectrometry of the oligosaccharides produced after hydrolysis of acetylated and nonacetylated rhamnogalacturonan. Oligomers esterified by an acetyl group on the reducing galacturonic acid residue or fully acetylated were detected in the hydrolysate showing that the novel enzyme is able to bind acetylated galacturonic acid in its active site. |
| doi_str_mv | 10.1007/s00253-009-2310-3 |
| format | Article |
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Oligomers esterified by an acetyl group on the reducing galacturonic acid residue or fully acetylated were detected in the hydrolysate showing that the novel enzyme is able to bind acetylated galacturonic acid in its active site.</description><subject>Acids</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Chromatography</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Liquid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. 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The activity was isolated by hydrophobic interaction chromatography, gel filtration, and preparative isoelectric focusing, resulting in the isolation of five different rhamnogalacturonan hydrolases exhibiting various isoelectric points from 6.2 to 7.7. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and mass spectrometry analyses after trypsin cleavage of the five fractions revealed that the five rhamnogalacturonases have a molar mass of 55 kDa without any divergences in the identified peptides. The RGase with a pI of 7.2 exhibited a pH optimum between 4.5 and 5 and a temperature optimum between 40°C and 50°C. Its mode of action was analyzed by mass spectrometry of the oligosaccharides produced after hydrolysis of acetylated and nonacetylated rhamnogalacturonan. 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| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2010-03, Vol.86 (2), p.577-588 |
| issn | 0175-7598 1432-0614 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Acids Biochemistry Biological and medical sciences Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Chromatography Chromatography, Gel Chromatography, Liquid Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes Fundamental and applied biological sciences. Psychology Fungal Proteins - isolation & purification Fungal Proteins - metabolism Glycoside Hydrolases - isolation & purification Glycoside Hydrolases - metabolism Hydrogen-Ion Concentration Isoelectric Focusing Isoelectric Point Life Sciences Mass Spectrometry Microbial Genetics and Genomics Microbiology Microbiology and Parasitology Mode of action Molecular Weight Oligosaccharides - metabolism Pectins - metabolism Peptides Polyporales - enzymology Proteins Scientific imaging Studies Sugar Temperature |
| title | Purification, characterization, and mode of action of a rhamnogalacturonan hydrolase from Irpex lacteus, tolerant to an acetylated substrate |
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