Purification, characterization, immobilization and applications of an enzybiotic β-1,3–1,4-glucanase produced from halotolerant marine Halomonas meridiana ES021

Abstract

Extracellular β-1,3–1,4-glucanase-producing strain Halomonas meridiana ES021 was isolated from Gabal El-Zeit off shore, Red Sea, Egypt. The Extracellular enzyme was partially purified by precipitation with 75% acetone followed by anion exchange chromatography on DEAE-cellulose, where a single protein band was determined with molecular mass of approximately 72 kDa. The Km value was 0.62 mg β-1,3–1,4-glucan/mL and Vmax value was 7936 U/mg protein. The maximum activity for the purified enzyme was observed at 40 °C, pH 5.0, and after 10 min of the reaction. β-1,3–1,4-glucanase showed strong antibacterial effect against Bacillus subtilis, Streptococcus agalactiae and Vibrio damsela. It also showed antifungal effect against Penicillium sp. followed by Aspergillus niger. No toxicity was observed when tested on Artemia salina. Semi-purified β-1,3–1,4-glucanase was noticed to be effective in clarification of different juices at different pH values and different time intervals. The maximum clarification yields were 51.61% and 66.67% on mango juice at 40 °C and pH 5.3 for 2 and 4 h, respectively. To our knowledge, this is the first report of β-1,3–1,4-glucanase enzyme from halotolerant Halomonas species. Graphic Abstract

Isolation of bacteria displaying potent antagonistic activity against fungi causes anthracnose disease in chili

“…Glucanolytic enzymes, namely 1,3-glucanase, are significant for the biological control of fungal pathogens because of their ability to degrade pathogen cell walls that contain 1,3glucan. So, β-1,3-glucanase and antifungal biocontrol bacterial strains are promising candidates for conventional antifungals (Gadallah et al 2023).…”