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Singh, A., Kuhad, R. C. and Ward, O. P. “Industrial application of microbial cellulases,” in Lignocellulose Biotechnologgy: Future Prospects, R. C. Kuhad and A. Singh, Eds., pp. 345-358, I.K.International Publishing House, New Delhi, India, 2007.

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Article

A Novel Cellulase from an Endophyte, Penicillium Sp. NFCCI 2862

1Microbial Biotechnology Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu Tawi, India


American Journal of Microbiological Research. 2013, Vol. 1 No. 4, 84-91
DOI: 10.12691/ajmr-1-4-4
Copyright © 2013 Science and Education Publishing

Cite this paper:
Saima Syed, Syed Riyaz-Ul-Hassan, Sarojini Johri. A Novel Cellulase from an Endophyte, Penicillium Sp. NFCCI 2862. American Journal of Microbiological Research. 2013; 1(4):84-91. doi: 10.12691/ajmr-1-4-4.

Correspondence to: Sarojini  Johri, Microbial Biotechnology Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu Tawi, India. Email: sjohri@iiim.ac.in

Abstract

An endophytic fungus identified as Penicillium sp. CPF2 (NFCCI 2862) was used to evaluate the activity of its cellulolytic enzymes to degrade pretreated sugarcane bagasse and characterize the cellulase enzymes. Different substrates were evaluated for optimum cellulase production by CPF2. The best activities for FPase (1.2 IU/ml), endocellulase (19 IU/ml), xylanase (40 IU/ml) and β-glucosidase (2.8 IU/ml) with a protein content of 0.86 mg/ml were observed when cellulose (1.5 % w/v) was used in combination with peptone (0.2 % w/v) in the growth medium. Optimum temperature and pH for the extracellular cellulase production were 28°C and 5.5, respectively. Furthermore the hydrolysis performance of Penicillium cellulase was compared with Trichoderma reesei cellulase (celluclast). Concentrated filtrate (~20 fold) from the fermented broth of CPF2 was able to bring about > 90 % and >63 % hydrolysis of cellulose and steam exploded bagasse (SEB) respectively at 5 % (w/v) substrate concentration in 24 h which was significantly higher than hydrolysis yield obtained with the commercial enzyme Celluclast.

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