| Autor: |
Simona Giacobbe, Olimpia Pepe, Valeria Ventorino, Leila Birolo, Roberto Vinciguerra, Vincenza Faraco |
| Jazyk: |
angličtina |
| Rok vydání: |
2014 |
| Předmět: |
|
| Zdroj: |
BioResources, Vol 9, Iss 3, Pp 4873-4887 (2014) |
| Druh dokumentu: |
article |
| ISSN: |
1930-2126 |
| DOI: |
10.15376/biores.9.3.4873-4887 |
| Popis: |
Pectinolytic enzymes play an important role in the processing of lignocellulosic materials because of their ability to improve the access of cellulases to their substrate by removing pectins. The strain Paenibacillus xylanolyticus 2-6L3 was isolated from mature compost obtained from agro-industrial wastes, and the enzyme pectate lyase from P. xylanolyticus 2-6L3, named PaenxylPel, was partially purified and subjected to structural and functional characterisation. The enzyme exhibited an optimum temperature between 60 and 70 °C and optimal pH value of 9.0 for its pectinase activity on pectin from citrus fruit. PaenxylPel showed a thermoresistance and pH resistance higher than those of other pectate lyases so far described, with half-lives of 48 and 24 h at 60 and 70 °C, respectively, a retention of around 80% of activity after 96 h at 40 and 50 °C, and a half-life of about 15 days at pH 8.0. PaenxylPel followed Michaelis-Menten kinetics toward pectin from citrus fruit, pectin from sugar beet pulp, high-ester pectin extracted from citrus peel (> 50% esterified), and polygalacturonic acid (PLA). The ability to act on both PLA and highly methylated pectins, together with a double peak in the graph of optimum pH at pH 5 and 9, suggest that pectate lyase from P. xylanolyticus shows an unusual activity, combining traits of pectate lyase and pectin lyase. This is the first manuscript on the pectinolytic activity of P. xylanolyticus. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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