Cloning, expression and characterization of a pectate lyase from Paenibacillus sp. 0602 in recombinant Escherichia coli

摘要: Biotechnological applications of microbial pectate lyases (Pels) in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process. Since Pels various fields widening, it is necessary to explore new pectolytic microorganisms and enzymes efficient effective usage. Here, we describe the cloning, expression, characterization application recombinant Pel protein from a bacterium genus Paenibacillus Escherichia coli. A gene (pelN) was cloned using degenerate PCR inverse chromosomal DNA sp. 0602. The open reading frame pelN encodes 30 amino acid signal peptide 445 mature belonging polysaccharide lyase family 1. maximum activity produced by E. coli shake flasks reached 2,467.4 U mL−1, purified enzyme exhibits specific 2,060 mg−1 on polygalacturonic (PGA). observed buffer with 5 mM Ca2+ at pH 9.8 65°C. PelN displays half-life around 9 h 42 h 50°C 45°C, respectively. biochemical treatment achieved maximal reduction percentage weight (30.5%) ramie bast fiber. This work represents first study that describes extracellular expression species high yield overexpression, relevant thermostability combined treatments indicate its strong potential large-scale industrial production.