RETRACTED:Screening and Characterization of Carboxymethyl Cellulase (CMCase) and Filter Paperase from Psychrophilic Fungus Truncatella angustata BPF5

Le résumé fourni par la source

This study characterized a novel cellulase-producing fungus, Truncatella angustata BPF5, isolated from Baramula, Jammu and Kashmir. Cellulase was produced in submerged fermentation using carboxymethyl cellulose (CMC) as substrate at pH 5, 20 °C, and 1% inoculum for five days. Reducing sugars were quantified by DNS assay. Filter paperase (FPase) showed maximum activity at 60 °C and pH 10, confirming it as an alkaliphilic metalloenzyme, strongly activated by Mn 2+ and Cu 2+ . FPase retained 100% activity with Tide detergent at 1% concentration, crude Carboxymethyl cellulase (CMCase) showed highest activity at 40 °C, pH 4.0, with 1% CMC, indicating an acidophilic nature. CMCase was also a Cu 2+ -activated metalloenzyme, retaining 100% activity with Surfexcel detergent at 1% concentration. The main finding is that CMCase is acidophilic while FPase is alkaliphilic, with Cu 2+ serving as a common activator. Both enzymes exhibited wide pH and temperature stability, making them promising for low-cost commercial production. To our knowledge, this is the first report on cellulase characterization from T. angustata BPF5. These cellulases show potential applications in cellulose hydrolysis for bioethanol production and in the detergent industry.

Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.