Finding Potential Source of Cold-Active Xylanase
Keywords:
Cold active xylanase, Xylan, Penicillium canesence, Truncatella angustata, Pseudogymnoascus roseus, ScreeningAbstract
Xylanases are glycosidases that catalyze the endohydrolysis of 1,4-β-D-xylosidic linkages in xylan, the main constituent of hemicelluloses found in plant cell wall. Xylanases encompass great industrial potential, and their cold-active counterparts have even more than that. Accordingly, three cold-active fungi, Penicillium canesence (BPF4), Truncatella angustata (BPF5), and Pseudogymnoascus roseus (BPF6) available as laboratory stocks have been screened for their ability to produce extracellular xylanases at cold temperature. The selection of hyper producing strains of xylanase was carried out on Potato Dextrose Agar (PDA) medium fortified with 1% (w/v) of xylan incubated at 20oC for seven days. Selection for best producer of xylanase was done on the basis of breadth of clear zones observed after flooding the plates with Gram’s iodine indicating the hydrolysis of xylan by xylanase around the colonies. The fungus T. angustata was found to produce the highest amount of xylanase followed by Pseu. roseus and P. canesence in that order. The cold-active xylanase-secreting ability of the fungal species was verified by incubating them in xylanase producing medium at 20oC. Consequently, T. angustata, Pseu. roseus and P. canesence were found to produce xylanase activity equal to 11.0 IU/ml, 7.0 IU/ml and 5.9 IU/ml respectively. This is the first report of the fungus T. angustata having cold-active xylanases producing ability.
References
M.M.H. Huisman, H.A. Schols, A.G.I. Voragem, “Glucuronoarabinoxylan from maize kernel cell walls are more complex than those from Sorghum kernel cell walls”, Carbohydrte Polymers, Vol. 43, Issue.3, pp.269-279, 2000.
D. Shallom, Y. Shoham, “Microbial hemicellulases”, Current Opinion in Microbiology, Vol.6, Issue.3, pp.219-228, 2003.
T. Collins, C. Gerday, G. Feller, “Xylanases, xylanase families and extremophilic xylanases”, FEMS Microbiology Reviews, Vol. 29, Issue.1, pp.3-23, 2005.
Q.K. Beg, M. Kapoor, L. Mahajan, G.S. Hoondal, “Microbial xylanases and their industrial applications”, Applied Microbiology and Biotechnology, Vol. 56, Issue.3-4, pp.326-338, 2001.
D. Haltrich, B. Nidetzky, K.D. Kulbe, W. Steiner, S. Zupancic, “Production of fungal xylanases”, Bioresource Technology, Vol. 58, Issue.2, pp.137-161, 1996.
K.K.Y. Wong, L.U.L. Tan, J.N. Saddler, “Multiplicity of 3-1,4-Xylanase in Microorganisms: Functions and Applications”, Microbiological Reviews, Vol. 52, Issue.3, pp.305-317, 1988.
P. Pellerin, M. Grosselin, J. Lepoutre, E. Samain, P. “Debeire, Enzymic production of oligosaccharides from corncob xylan”, Enzyme and Microbial Technology, Vol. 13, Issue.8, pp.617-621, 1991.
P. Biely, “Microbial xylanolitic systems”, Trends in Biotechnology, Vol. 3, Issue.1, pp.286-295, 1985.
L.E.A. Pucci, P.B. Rodrigues, P. Borges, R.T.F. Freitas, “Oil levels and enzymatic complex addition in broiler diets”, Revista Brasileira de Zootecnia, Vol. 32, Issue.4, pp.909-917, 2003.
S. Sahay, B. Hamid, P. Singh, K. Ranjan, D. Chauhan, R.S. Rana, V.K. Chaurse, “Evaluation of pectinolytic activities for oenological uses from psychrotrophic yeasts”, Letters in Applied Microbiology, Vol.. 57, Issue.2, pp.115-121, 2013.
S. Kar, A. Mandal, P.K. Mohapatra, K.C. Mondal, B.R. Pati, “Production of cellulase-free xylanase by Trichoderma reesei SAF3”, Brazilian Journal of Microbiology, Vol. 37, Issue.4, pp.462-464, 2006.
G. Narasimha, A. Sridevi, V. Buddolla, M.C. Subhosh, B.R. Rajasekhar, “Nutrient effects on production of cellulolytic enzymes by Aspergillus niger”, African Journal of Biotechnology, Vol. 5, Issue. 5, pp.472–476, 2006.
D. Chouhan, S. Sahay, “Detergent compatible cold-active lipases from psychrotrophic fungi for cold washing”, Journal of Genetic Engineering and Biotechnology. (in press), 2018.
P. Singh, B. Hamid, M.A. Lone, K. Ranjan, A. Khan, V.K. Chaurse., S. Sahay, “Evaluation of pectinonase activity from the psychrophilic fungal strain Truncatella angustata –BPF5”, Journal of Endocytobiosis and Cell Research, Vol. 22, pp.57-61, 2012.
S. Nakamura, K. Wakabayashi, R. Nakai, R. Aono, K. Horikoshi, “Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. Strain 41 M-1”, Applied and Environmental Microbiology, Vol. 59, Issue.7, pp.2311-2316, 1993.
M.J.Bailey, P. Biely, K. Poutanen, “Interlaboratory testing of methods for assay of xylanase activity”, Journal of Biotechnology, Vol. 23, Issue.3, pp.257–270, 1992.
G.L. Miller, “Use of dinitrosalicylic acid reagent for determination of reducing sugar”, Analytical chemistry, Vol. 31, Issue.3, pp.426-428, 1959.
L. Fengxia, L. Mei, L. Zhaoxin, B. Xiaomei, Z. Haizhen, W. Yi, “Purification and characterization of xylanase from Aspergillus ficuum AF-98”, Bioresource Technology, Vol. 99, Issue.13, pp.5938-5941, 2008.
O. Martin Jeremy, Torres, E. Thomas Edison, dela Cruz, “Production of xylanases by mangrove fungi from the Philippines and their application in enzymatic pretreatment of recycled paper pulps”, World Journal of Microbiology and Biotechnology, Vol. 29, Issue.4, pp.645-655, 2013.
D. Garai, V. Kumar, “Response surface optimization for xylanase with high volumetric productivity by indigenous alkali tolerant Aspergillus candidus under submerged cultivation”, Biotech, Vol. 3, Issue.2, pp.127-136, 2013.
C.C. Lee, M. Smith, R.E. Kibblewhite-Accinelli, “Isolation and characterization of a cold-active xylanase enzyme from Flavobacterium sp”, Current Microbiology, Vol. 52, Issue.2, pp.112-116, 2006.
B. Guo, X.L. Chen, C.Y. Sun, B.C. Zhou, Y.Z. Zhang, “Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1, 4-xylanase from marine Glaciecola mesophila KMM 241”, Applied Microbiology and Biotechnology, Vol. 84, Issue.6, pp.1107-1115, 2009.
G. Wang, H. Luo, Y. Wang, H. Huang, P. Shi, P. Yang, B. Yao, “A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization”, Bioresource Technology, Vol. 102, Issue.3, pp.3330-3336, 2011.
J. Zhou, Y. Dong, X. Tang, “Molecular and biochemical characterization of a novel intracellular low-temperature active xylanase”, Journal of Microbiology and Biotechnology, Vol. 22, Issue.4, pp.501-509, 2012.
X. Liu, Z. Huang, X. Zhang, Z. Shao, Z. Liu, “Cloning, expression and characterization of a novel cold-active and halophilic xylanase from Zunongwangia profunda”, Extremophiles, Vol. 18, Issue.2, pp.441-450, 2014.
S.Y. Wang, W. Hu, X.Y. Lin, “A novel cold-active xylanase from the cellulolytic myxobacterium Sorangium cellulosum So9733-1: gene cloning, expression, and enzymatic characterization”, Applied Microbiology and Biotechnology, Vol. 93, Issue.4, pp.1503-1512, 2011.
G. Garg, S.S. Dhiman, R. Mahajan, A. Kaur, J. Sharma, “Bleach-boosting effect of crude xylanase from Bacillus stearothermophilus SDX on wheat straw pulp”, New Biotechnology, Vol. 28, Issue.1, pp.58-64, 2011.
L.N. Twomey, J.R. Pluske, J.B. Rowe, M. Choct, W. Brown, M.F. McConnell, D.W. Pethick, “The effects of increasing levels of soluble non-starch polysaccharides and inclusion of feed enzymes in dog diets on faecal quality and digestibility”, Animal Feed Science and Technolology, Vol. 108, Issue.1-4, pp.71-82, 2003.
I. Romanowska, J. Polak, S. Bielecki, “Isolation and properties of Aspergillus niger BT-90 xylanase for bakery”, Applied Microbiology and Biotechnology, Vol. 69, Issue.6, pp.665-671, 2006.
S. Albert, D. Chauhan, B. Pandya, A. Padhiar, “Screening of Trichoderma spp.as potential fungal partner in co-culturing with white rot fungi for efficient biopulping”, Global J. Biotechnol Biochem, Vol. 6, Issue.3, pp.95-101, 2011.
Y. Sun, J. Cheng, “Hydrolysis of lignocellulosic materials for ethanol production: a review”, Bioresource Technology, Vol. 83, Issue.1, pp.1-11, 2002.
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