Comparative production of cellulases by mutants of Penicillium janthinellum NCIM 1171 and its application in hydrolysis of Avicel and cellulose

• Published in: Bioresource technology Vol. 102; no. 11; pp. 6569 - 6572
• Main Authors: Singhvi, M.S., Adsul, M.G., Gokhale, D.V.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.06.2011; Elsevier
• Subjects: beta-Glucosidase - metabolism; Biological and medical sciences; Biotechnology; Cellulase; Cellulases - biosynthesis; Cellulose; Cellulose - metabolism; Enzyme Stability; Enzymes; Fermentation; Fundamental and applied biological sciences. Psychology; Hydrolysis; Inactivation; Methods. Procedures. Technologies; Microbial engineering. Fermentation and microbial culture technology; Mutant EU2D-21; Mutation - genetics; Penicillium - enzymology; Penicillium - genetics; Penicillium janthinellum; Solid state fermentation; Submerged fermentation; Substrate Specificity; Temperature; Thermosensitive; β-Glucosidase thermostability; Submerged fermentation; β-Glucosidase thermostability; Mutant EU2D-21; Solid state fermentation; Enzyme; Cellulose; Thermal stability; Fungi; Glycosylases; Hydrolysis; β-Glucosidase; Cellulolytic enzyme; Submerged culture; Cellulase; Glycosidases; Hydrolases; Solid substrate fermentation; Fungi Imperfecti; Mutation; Penicillium janthinellum
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2011.01.014

Mutants of Penicillium janthinellum NCIM 1171 were evaluated for cellulase production using both submerged fermentation (SmF) and solid state fermentation (SSF). Mutant EU2D-21 gave highest yields of cellulases in both SmF and SSF. Hydrolysis of Avicel and cellulose were compared using SmF and SSF derived enzyme preparations obtained from EU2D-21. Surprisingly, the use of SSF derived preparation gave less hydrolysis compared to SmF derived enzymes. This may be due to inactivation of β-glucosidase at 50°C in SSF derived enzyme preparations. SmF derived enzyme preparations contained both thermostable and thermosensitive β-glucosidases where as SSF derived enzyme preparations contained predominantly thermosensitive β-glucosidase. This is the first report on less thermostability of SSF derived β-glucosidase which is the main reason for getting less hydrolysis.