An insight into the lignin peroxidase of Macrophomina phaseolina

Abstract

Macrophomina phaseolina is one of the deadliest necrotrophic fungal pathogens that infect more than 500 plant species including major food, fiber, and oil crops all throughout the globe. It secretes a cocktail of ligninolytic enzymes along with other hydrolytic enzymes for degrading the woody lignocellulosic plant cell wall and penetrating into the host tissue. Among them, lignin peroxidase has been reported only in Phanerochaete chrysosporium so far. But interestingly, a recent study has revealed a second occurrence of lignin peroxidase in M. phaseolina. However, lignin peroxidases are of much significance biotechnologically because of their potential applications in bio-remedial waste treatment and in catalyzing difficult chemical transformations. Besides, this enzyme also possesses agricultural and environmental importance on account of their role in lignin biodegradation. In the present work, different properties of the lignin peroxidase of M. phaseolina along with predicting the 3-D structure and its active sites were investigated by the use of various computational tools. The data from this study will pave the way for more detailed exploration of this enzyme in wet lab and thereby facilitating the strategies to be designed against such deadly weapons of Macrophomina phaseolina. Furthermore, the insight of such a ligninolytic enzyme will contribute to the assessment of its potentiality as a bioremediation tool.

Keywords: Ligin peroxidase; Macrophomina phaseolina; lignin.

Figure 1

Methodolgy involved in characterisation of M. phaseolina.

Figure 2

Conserved domain over lignin peroxidase

Figure 3

The final 3D structure of lignin peroxidase model from Macrophomina phaseolina. The α-helices and β –sheets are represented by redhelices and yellow ribbons respectively. This model was conducted by Phyre2 MODELLER program.

Figure 4

Ramachandran's Map of lignin peroxidase model from Macrophomina phaseolina. The Plot calculation was done with PROCHECK program

Figure 5

a) Active site information by CASTp. Green color shows the active site position from 76 to 287 with the β-sheet in between them and 3D representation of the best active site of lignin peroxidase generated by using CASTp; b) The table shows the area and the volume for different active sites of lignin pefroxidase and the best active site remains in an area of 1027 and a volume of 1359.9 amino acid.