American Journal of Microbiological Research
ISSN (Print): 2328-4129 ISSN (Online): 2328-4137 Website: https://www.sciepub.com/journal/ajmr Editor-in-chief: Apply for this position
Open Access
Journal Browser
Go
American Journal of Microbiological Research. 2013, 1(4), 84-91
DOI: 10.12691/ajmr-1-4-4
Open AccessArticle

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

Saima Syed1, Syed Riyaz-Ul-Hassan1 and Sarojini Johri1,

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

Pub. Date: November 08, 2013

Cite this paper:
Saima Syed, Syed Riyaz-Ul-Hassan and 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

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.

Keywords:
Penicillium sp. cellulase endophyte extracellular sugarcane bagasse

Creative CommonsThis work is licensed under a Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

Figures

Figure of 6

References:

[1]  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.
 
[2]  Kuhad, R. C., Gupta, R. and Singh, A., “Microbial Cellulases and Their Industrial Applications”, 2011, Enzyme Research, Article ID 280696.
 
[3]  Lynd, L. R., Weimer, P. J., Vanzyl, W. H. and Pretorius, J. S., “Microbial cellulose utilization: fundamentals and biotechnology” Microbiology and Molecular Biology Reviews, 66. 506-577. 2002.
 
[4]  Bhat, M. and Bhat, S, “Cellulose degrading enzymes and their potential industrial applications,” Biotechnology Advances, 15. 583-620. 1997.
 
[5]  Wood, T. M., “Mechanisms of cellulose degradation by enzymes from aerobic and anaerobic fungi. In: Enzyme systems for lignocellulose degradation” NY: Elsevier;, pp. 1. 1989.
 
[6]  Tolan, J. S. and Foody, B., “Cellulases from submerged fermentation,” Advances in Biochemical Engineering Biotechnology, 65. 41-67. 1999.
 
[7]  Duff, S. J. B., Murray, W. D., “Bioconversion of forest products industry waste cellulosics to fuel ethanol: a review,” Bioresource Technology, 55. 1-33. 1996.
 
[8]  Brown, J. A., Collin, S. A. and Wood, T, M., “Development of a medium for high cellulase, xylanase and β-glucosidase production by a mutant strain (NTG III/6) of the cellulolytic fungus Penicillium pinophilum,” Enzymes and Microbial Technology, 9. 355-360. 1987.
 
[9]  Krogh, K. B. R., Mørkeberg, A., Jørgensen, H., Frisvad, J. C. and Olsson, L. “Screening genus Penicillium for producers of cellulolytic and xylanolytic enzymes,” Applied Biochemistry Biotechnology, 116. 389-401. 2004.
 
[10]  Strobel, G. A., Daisy, B., Castillo, U. and Harper, J., “Natural products from endophytic microorganisms,” Journal of Natural Products, 67. 257-268. 2004.
 
[11]  Shoseyov, O., Doi, R. H., “Essential 170-kDa subunit for degradation of crystalline cellulose by Clostridium cellulovorans cellulose,” Proceedings of the National Academy of Sciences USA, 87. 2192-2195. 1990.
 
[12]  Saghai-Maroof, M. A., Soliman, K. M., Jorgensen, R. A. and Allard, R. W., “Ribosomal spacer length polymorphisms in barley: Mendelian inheritance, chromosomal location and population dynamics” Proceedings of the National Academy of Sciences USA, 81. 8014-8019. 1984.
 
[13]  Mandels, M., Sternburg, D., “Recent advances in cellular technology,” Journal of Fermentation Technology, 54. 267-286. 1976.
 
[14]  Ghose, T. K., “Measurement of cellulase activites” Pure and Applied Chemistry, 59. 257-268. 1987.
 
[15]  Bradford, M. M., “A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, 72. 227-254. 1976.
 
[16]  Hari, K. S., Prasanthi, K., Chowdary, G. V. and Ayyanna, C., “Simultaneous saccharification and fermentation of pretreated sugar cane leaves to ethanol,” Process Biochemistry, 33. 825-830. 1998.
 
[17]  Sieber, T. N., Sieber-Canavesi, F. and Dorworth, C. E., “Endophytic fungi of fungi alder (Alnus rubra) leaves and twigs in British Columbia,” Canadian Journal of Botany, 69. 407-411. 1991.
 
[18]  Carroll, G. C., Petrini, G. C. and Petrini, O., “Patterns of substrate utilization by some endophytes from coniferous foliage,” Mycologia, 75. 53-63. 1983.
 
[19]  Jorgensen, H., Morkeberg, A., Krogh, K. B. R. and Olsson, L., “Production of cellulases and hemicellulases by three Penicillium species: effect of substrate and evaluation of cellulase adsorption by capillary electrophoresis,” Enzymes and Microbial Technology, 36. 42-48. 2005.
 
[20]  Jorgensen, H. and Olsson, L., “Production of cellulases by Penicillium brasilianum IBT 20888 : Effect of substrate on hydrolytic performance,” Enzymes and Microbial Technology, 38. 381-390. 2006.
 
[21]  de Castro, A. M., de Albuquerque, de Carvalho, M. L., Leite, S. G., Pereira, N. J., “Cellulases from P. funiculosum: production, properties and application to cellulose hydrolysis,” Journal of Industrial Microbiology Biotechnology, 37. 151-158. 2010.
 
[22]  Henriksson, G., Johansson, G. and Pettersson, G., “A critical review of cellobiose dehydrogenases,” Journal of Biotechnology, 78. 93-113. 2000.
 
[23]  Wymelenberg, A. V., Sabat, G., Martinez, D., Rajangam, A. S., Teeri, T. .T. and Gaskell, J., “The P. chrysosporium secretome: Database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium Journal of Biotechnology, 118. 17-34. 2005.
 
[24]  Spiridonov, N. A. and Wilson, D. B., “Regulation of Biosynthesis of Individual cellulases in Thermomonospora fusca,” Journal of Bacteriology, 180. 3529-3532. 1998.
 
[25]  Garg, S. K. and Neelakantan, S., “Effect of cultural factors on cellulase activity and protein production by Aspergillus terreus,” Biotechnology and Bioengineering, 23. 1653-1659. .1981.
 
[26]  Adsul, M. G., Bastawde, K. B., Varma, A. J. and Gokhale, D. V., “Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulose production,” Bioresource Technology, 98. 1467-1473. 2007.
 
[27]  Brown, J. A., Collin, S. A., Wood, T. M., “Development of a medium for high cellulase, xylanase and β-glucosidase production by a mutant strain (NTG III/6) of the cellulolytic fungus Penicillium pinophilum,” Enzymes and Microbial Technology, 9. 355-360. 1987.