Pectinolytic enzymes have 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 xylanilyticus 2-6L3 was isolated from mature compost obtained from agro-industrial wastes, and the enzyme pectate lyase from P. xylanilyticus 2-6L3, named Paenxyl Pel, 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. Paenxyl Pel 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. Paenxyl Pel 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. xylanoliticus shows an unusual activity, combining traits of pectate lyase and pectin lyase. This is the first manuscript on the pectinolytic activity of P. xylanilyticus.

Identification and Characterisation of a Pectinolytic Enzyme from Paenibacillus xylanolyticus / Giacobbe, Simona; Pepe, Olimpia; Ventorino, Valeria; Birolo, Leila; Roberto, Vinciguerra; Faraco, Vincenza. - In: BIORESOURCES. - ISSN 1930-2126. - 9:3(2014), pp. 4873-4887.

Identification and Characterisation of a Pectinolytic Enzyme from Paenibacillus xylanolyticus

GIACOBBE, SIMONA;PEPE, OLIMPIA;VENTORINO, VALERIA;BIROLO, LEILA;FARACO, VINCENZA
2014

Abstract

Pectinolytic enzymes have 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 xylanilyticus 2-6L3 was isolated from mature compost obtained from agro-industrial wastes, and the enzyme pectate lyase from P. xylanilyticus 2-6L3, named Paenxyl Pel, 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. Paenxyl Pel 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. Paenxyl Pel 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. xylanoliticus shows an unusual activity, combining traits of pectate lyase and pectin lyase. This is the first manuscript on the pectinolytic activity of P. xylanilyticus.
2014
Identification and Characterisation of a Pectinolytic Enzyme from Paenibacillus xylanolyticus / Giacobbe, Simona; Pepe, Olimpia; Ventorino, Valeria; Birolo, Leila; Roberto, Vinciguerra; Faraco, Vincenza. - In: BIORESOURCES. - ISSN 1930-2126. - 9:3(2014), pp. 4873-4887.
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