Dual activity of Meloidogyne incognita-regulated Musa acuminata Pathogenesis-related-10 (MaPR-10) gene.

Plant immunity to pathogen infections is a dynamic response that involves multiple organelles and defence signalling systems such as hypersensitive response (HR) and systemic acquired resistance (SAR). The latter requires the function of Pathogenesis-related (PR) proteins, a common plant protein family with diverse roles in plant innate immunity. Our previous proteomics study showed that a PR gene (ITC1587_Bchr9_P26466_MUSBA) was differentially regulated during a compatible banana-M. incognita interaction, substantiating the isolation of this gene in the current study. Here, we successfully isolated and characterised Pathogenesis-related-10 (PR10) gene with ß-1,3-glucanase and ribonuclease (RNase) activities from two Musa acuminata cultivars (denoted as MaPR10) namely Berangan and Grand Naine (ITC1256). We found that MaPR10 cloned sequences possess glycine-rich loop domain and shared conserved motifs specific to PR10 gene group, confirming its identity as a member of this group. Interestingly, we also found a catalytic domain sequence for glycoside hydrolase family 16 (EXDXXE), unique only to MaPR10 cloned sequences. Two peptide variants closely related to the reference sequence ITC1587_Bchr9_P26466_MUSBA namely MaPR10-BeB5 and MaPR10-GNA5 were overexpressed and purified to test for their functionality. Here, we confirmed that both protein variants possess ß-1,3-glucanase and ribonuclease (RNase) activities, and inhibit the growth of Aspergillus fumigatus, a human opportunistic pathogen. To our knowledge, this is the first PR10 plant proteins with such properties to be reported thus far.

Mixing of Prosopis africana pods and corn cob exerts contrasting effects on the production and quality of Bacillus thuringiensis crude endoglucanase.

Recently, attention has shifted to the use of mixed lignocellulosic substrates for the production of cellulolytic enzymes. However, researchers have focused mainly on achieving increased enzyme yields while neglecting other properties of the enzymes when using such mixtures. In this first-ever report of the application of Prosopis africana pod (PAP) in cellulase production, we investigated the effect of its combination with corn cob (CC), as an inducing carbon source, on the amounts and quality of crude endoglucanase produced by Bacillus thuringiensis SS12. The organism was grown on PAP, CC or their 1:1% w/w mixture (MS) and the crude endoglucanases produced were tested for activity, hydrolytic efficiency, and thermostability. PAP supported the highest enzyme activity (0.138 U/mL) and its endoglucanase was the most effective in hydrolyzing CMC and filter paper while CC-derived endoglucanase was the best for hydrolysis of alkali-pretreated CC. Enzyme activity of MS-derived endoglucanase (0.110 U/mL) was intermediate to that of PAP and CC (0.091 U/mL) and was the most stable at elevated temperatures (70 and 80 °C). It also liberated the least amount of reducing sugars from all tested substrates. Combination of both the substrates, thus, favored enzyme production and thermostability but was detrimental to hydrolytic efficiency.