Characterization of Two Paenibacillus amylolyticus Strain 27C64 Pectate Lyases with Activity on Highly Methylated Pectin

Abstract

Two pectate lyases were identified from Paenibacillus amylolyticus 27C64; both enzymes demonstrated activity on methylated pectin in addition to polygalacturonic acid. PelA is in a subclass of the pectate lyase family III. PelB shows some features of pectate lyase family I but is highly divergent.Pectinases have many industrial applications, including uses in food and textile production (9, 12). Additionally, pectinases are important for the degradation of biomass, where pectin can comprise a significant portion of plant structure (5, 6). The degradation of pectin requires methylesterases and depolymerases. Pectin methylesterases are responsible for the hydrolysis of methylester linkages from the polygalacturonic acid (PGA) backbone (24), while pectin depolymerases act upon the polygalacturonate backbone and belong to one of two families, polygalacturonases or lyases. Polygalacturonases hydrolytically cleave the polygalacturonate chain, while lyases cleave by ␤-elimination, giving a ⌬4,5-unsaturated product (10, 19). There are two types of lyases: pectate lyases (PLs), which cleave unesterified polygalacturonate, and pectin lyases, which cleave methylesterified pectin.Paenibacillus amylolyticus strain 27C64, isolated from the larval hindgut of the aquatic crane fly, Tipula abdominalis, possesses a wide range of lignocellulose-degrading enzymes. This study describes two pectate lyases from P. amylolyticus that display unusual activity by combining traits of pectate and pectin lyases (2,7,21,22).Identification of pelA and pelB. A library containing 2-to

Identification and Characterisation of a Pectinolytic Enzyme from Paenibacillus xylanolyticus

“…These results are in agreement with those on other pectate lyases published by Soriano et al (2000) and Boland et al (2010). Soriano et al (2000) studied pelA, from the strain Paenibacillus sp.…”

“…BP-23, actives on pectins of any degree of esterification. Boland et al (2010) described two pectinases from P. amylolyticus, PelA and PelB, that are pectate lyases that show a remarkable pectin lyase activity. The peculiar double peak observed in the graph of optimum pH at (pH 9 and 5) for PaenxylPel can be explained by the ability of the enzyme to work as both pectate lyase, typically characterised by optimum alkaline pH, and pectin lyase, typically exhibiting an optimum acidic pH.…”

Improving the thermoactivity and thermostability of pectate lyase from Bacillus pumilus for ramie degumming

“…Therefore, thermostable enzymes that have high catalytic activity under alkaline conditions are desirable for industrial degumming applications. For this purpose, alkaline Pels have been cloned from microbes (Berensmeier et al 2004;Boland et al 2010;Hatada et al 2001;Li et al 2014;Tardy et al 1997;Wang et al 2014;Zhang et al 2013) or from metagenomic DNA obtained from alkaline environment soils . In this study, BpPel from B. pumilus (ATCC 7061) was successfully engineered to improve its catalytic activity and thermostability for potential industrial application for ramie degumming process.…”

Expression and thermostability of Paenibacillus campinasensis BL11 pectate lyase and its applications in bast fibre processing

“…This is the first time a gene encoding a 35.6 kDa pectate lyase was identified from P. campinasensis . There were just only two previous works investigating pectate lyases from Paenibacillus species (Soriano et al , 2006; Boland et al , 2010). The deduced amino acid sequence is very different from the sequences of all other pectate lyases listed in the database, except that of Bacillus sp.…”