Mode of action of Bacillus licheniformis pectin methylesterase on highly methylesterified and acetylated pectins
| Autor: | Hans Christian Buchholt, Henk A. Schols, Bruno M. Moerschbacher, Martin Wagenknecht, Harry Gruppen, C.A. Remoroza |
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| Rok vydání: | 2015 |
| Předmět: |
aspergillus-niger
animal structures food.ingredient Polymers and Plastics Pectin sugar-beet pectins Molecular Sequence Data Sequence Homology Bacillus de-esterification medicine.disease_cause complex mixtures Esterase food Bacterial Proteins Levensmiddelenchemie Escherichia coli Materials Chemistry medicine environmental-conditions Amino Acid Sequence Bacillus licheniformis methyl esterase VLAG degradation chemistry.chemical_classification calcium Food Chemistry Esterification biology Organic Chemistry Aspergillus niger food and beverages Acetylation biology.organism_classification Pectinesterase Enzyme chemistry Biochemistry esterified oligogalacturonides escherichia-coli Pectins Beta vulgaris Carboxylic Ester Hydrolases Sequence Alignment structural features |
| Zdroj: | Carbohydrate Polymers 115 (2015) Carbohydrate Polymers, 115, 540-550 |
| ISSN: | 0144-8617 |
| DOI: | 10.1016/j.carbpol.2014.09.016 |
| Popis: | A gene encoding a putative pectinesterase from Bacillus licheniformis DSM13 was cloned and expressed in Escherichia coli. The resulting recombinant enzyme ( Bli PME) was purified and characterized as a pectin methylesterase. The enzyme showed maximum activity at pH 8.0 and 50 °C. Bli PME is able to release up to 100% of the methylesters from lime pectin (DM 34–76 → DM 0) and up to 73% of all methylesters from SBPs (DM 30–73 → DM 14). Bli PME efficiently de-methylesterifies lemon pectins and SBPs in a blockwise manner and is quite tolerant towards the acetyl groups present within the SBPs. Detailed analysis of the Bli PME-modified pectins using HILIC–MSn and the classical calcium reactivity measurement showed that the enzyme generates pectins with low methylesterification (lime and SBP) and high acetyl content (SBP) while creating blocks of nonmethylesterified galacturonic acid residues. The high activity of Bli PME towards highly methylesterified and acetylated pectins makes this novel esterase more efficient in removing methylesters from highly esterified beet pectin compared to other PMEs, e.g. Aspergillus niger PME. |
| Databáze: | OpenAIRE |
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