Screening and optimization of pectin lyase and polygalacturonase activity from ginseng pathogen Cylindrocarpon Destructans

Abstract

Cylindrocarpon destructans isolated from ginseng field was found to produce pectinolytic enzymes. A Taguchi's orthogonal array experimental design was applied to optimize the preliminary production of polygalacturonase (PG) and pectin lyase (PL) using submerged culture condition. This method was applied to evaluate the significant parameters for the production of enzymes. The process variables were pH, pectin concentration, incubation time and temperature. Optimization of process parameters resulted in high levels of enzyme (PG and PL) production after ten days of incubation at a pH of 5.0 at 25°C in the presence of 1.5% pectin. Among different nitrogen sources, urea and peptone showed high production of PG and PL, respectively. The enzyme production and mycelial growth seems to have direct influence on the culture conditions; therefore, at stationary state high enzyme production and mycelial growth were obtained than agitation state. Along with this, optimization of enzyme activity was also determined using various physiological parameters like, temperature, incubation time and pH. Taguchi's data was also analyzed using one step ANOVA statistical method

A Novel Endophytic Trichoderma longibrachiatum WKA55 With Biologically Active Metabolites for Promoting Germination and Reducing Mycotoxinogenic Fungi of Peanut

“…Pectin lyases (EC 4.2.2.2) are another enzyme that split the chain by removing a molecule of water from the linkage, releasing unsaturated double-bond products. The synergistic action of both enzymes breaks the pectin chain and releases a single unit of galacturonan (Sathiyaraj et al, 2011), leading to weakening of the cell walls and tissue maceration (liquefaction) thus development of many diseases, particularly those characterized by soft-rotting of tissues. This enzyme system is involved in many phytopathogens that invade the plant tissue (Rahman and Punja, 2005;Al-Askar et al, 2021a).…”

A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind’s Challenges

“…Normally, lyases have very limited substrate specificity; however, the independence of expensive cofactors encourages their commercial applications in many industries. One of the most reported lyases is pectin lyase catalyzes random degradation of pectin through the elimination of water molecules yielding one unite of galacturonan with unsaturated double bonds [142]. Pectin lyase plays a major role in fungal pathogenicity, though degrading the pectic materials holding the plant cell wall together [142].…”

“…One of the most reported lyases is pectin lyase catalyzes random degradation of pectin through the elimination of water molecules yielding one unite of galacturonan with unsaturated double bonds [142]. Pectin lyase plays a major role in fungal pathogenicity, though degrading the pectic materials holding the plant cell wall together [142]. The role of pectin lyase in fungal pathogenicity was reported in many plant pathogenic fungi, such as Clonostachys rosea [143], Cylindrocarpon destructans [142], and Penicillium canescens [144].…”

“…Pectin lyase plays a major role in fungal pathogenicity, though degrading the pectic materials holding the plant cell wall together [142]. The role of pectin lyase in fungal pathogenicity was reported in many plant pathogenic fungi, such as Clonostachys rosea [143], Cylindrocarpon destructans [142], and Penicillium canescens [144]. Alginate lyase represents another important fungal lyase; it catalyzes the degradation of alginate to defined oligosaccharides.…”