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Pectin lyase (PNL) is an important enzyme of the pectinases group which degrades pectin polymer to 4,5-unsaturated oligogalacturonides by a unique β-elimination mechanism and is used in several industries. The existence of multigene families of pectin lyases has been investigated by mining microbial genomes. In the present study, 52 pectin lyase genes were predicted from sequenced six species of Fusarium, namely F. fujikuroi, F. graminearum, F. proliferatum, F. oxysporum, F. verticillioides and F. virguliforme. These sequences were in silico characterized for several physico-chemical, structural and functional attributes. The translated PNL proteins showed variability with 344–1142 amino acid residues, 35.44–127.41 kDa molecular weight, and pI ranging from 4.63 to 9.28. The aliphatic index ranged from 75.33 to 84.75. Multiple sequence alignment analysis showed several conserved amino acid residues and five distinct groups marked as I, II, III, IV, and V were observed in the phylogenetic tree. The Three-dimensional Structure of five of these PNLs, each representing a distinct group of phylogenetic trees was predicted using I-TASSER Server and validated. The pectin lyase proteins of Fusarium species revealed close similarity with pectin lyase of Aspergillus niger PelA(1IDJ) and PelB(1QCX). Diversity in the structural motifs was observed among Fusarium species with 2 β-sheets, 1 β-hairpin, 7–12 β bulges, 18–25 strands, 6 -11 helices, 1 helix-helix interaction, 32–49 β turns, 2–6 γ turns and 2- 3 disulfide bonds. The unique Pec_lyase domain was uniformly observed among all PNL proteins confirming its identity. The genome-wide mining of Fusarium species was attempted to provide the diversity of PNL genes, which could be explored for diverse applications after performing cloning and expression studies. [ABSTRACT FROM AUTHOR]

Pectin, also known as pectic compounds, is a fundamental component of plant cell walls that imparts rigidity and structure. Pectin lyases have a unique β-elimination mechanism of directly degrading pectin polymers to 4, 5-unsaturated oligogalacturonides, while other pectinases have preferences for sequential degradation. Members of the pectin lyase family have characteristic Pec_Lyase_C domain and β-helix structure. They have been successfully isolated and characterized from different bacteria, fungi, and yeast. Based on their biochemical properties, pectin lyase is one of the most important enzymes in the commercial sector. In the current biotechnological world, these enzymes play a massive role in juice processing industries, retting of fibres, biosurfactant production, and they possess a biocontrol effect. Pectin lyases are promising for the fruit juice industry as they maintain the typical odor of juice and do not form extremely harmful methanol as a by-product. Several recent innovations related to production, purification, and molecular insights have been reported since the last review published by our group in 2009. This review is an attempt to update the sources, production strategies, biochemical attributes, molecular and expression profiling, bioinformatics, and genomic-driven research exclusively in pectin lyases. • Pectin lyases have a unique β-elimination mechanism of directly degrading pectin. • Microbes are the major sources of Pectin lyases. • Pectin lyases are used in juice industries, retting of fibres, and biosurfactant production. • Productions, purifications, and molecular studies on pectin lyase attempted. [ABSTRACT FROM AUTHOR]