LAUSR

Proteases are major group of industrial enzymes and account for approximately 60% of overall enzyme market and about 40% sale is reported total worldwide enzymes. In the present study, protease was isolated from Cheotomium globusum, then statistically optimized, characterized, purified and finally immobilized. Cheotomium globusum gave maximum yield (520.16 ± 1.6 U/mL) when grown on Vachellia nilotic (Kikar) while, the physical and nutritional parameters was optimized by Response Surface Methodology (RSM). The maximum protease activity (767.496 ± 3.5 U/mL) was achieved at pH 8, temperature 45 °C, time period 1 day, 5 mL of substrate and 5 mL inoculum size. A purification fold of 3.48 was achieved along with 321 U/mg specific activities while 4.5% yield was obtained after purification. The CHI-immobilized protease showed the stability in the alkaline pH range of 8–9 at 60 °C. Moreover, the CHI-immobilized protease showed significant stability up to 8 cycles of reuse. The pH and temperature stability of novel protease including its reusability makes it a very significant for commercial use. In conclusion, the protease produced from lignocellulosic substrates by Cheotomium globusum through SSF showed its potential in feathers degradation and Gelatin layer decomposition from X-ray film and detergent industry. The enzyme produced from lignocellulosic agro waste via the proposed optimized biotechnological process can be explored for multiple industrial applications.