Different methods and carriers for immobilization cellulase from Trichoderma viride and its remaining activity

Abdul Sattar Jabbar Taha


Objective: Many methods for enzymes immobilization and large number of carriers for immobilized enzymes, there are many benefits and diffeculties for immobilization, so the objective of this paper is to determine the suitable method and carrier for cellulase immobilization.

Methods: Three methods used for immobilization which they adsorption, Glutaraldehyde and modified glutaraldehyde using two different carriers the first anion exchanger AM-21-A, and the second cation exchange fiber VION KN -1.

Results: The result shows that the degree of saving catalytic activity for immobilized and free cellulase were 35, 55, and 75% for the three methods respectively and The result of degree maintain of specific activity for native enzyme were 57%, 42%, for the two carriers VION KN-1, AM-21-A respectively.

Conclusions: It can be concluded that the modified glutaraldehyde is the best method for cellulase immobilization and VION KN-1 is better carrier than AM-21-A.


Immobilization cellulase, Adsorption, Glutaraldehyde, Modified Glutaraldehyde, Remaining activity, VION KN-1, AM-21-A

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Cerveró JM, Skovgaard PA, Felby C, Sørensen HR, Jørgensen H. Enzymatic hydrolysis and fermentation of palm kernel press cake for production of bioethanol. Enzyme Microb Technol. 2010;46(3-4):177–84.

Sheldon RA. Enzyme immobilization: the quest for optimum performance. Adv Synth Catal. 2007;349(8–9):1289–307.

Cass T, Ligler FS. Immobilized biomolecules in analysis: a practical approach. Practical approach series. Oxford University Press, New York; 1999.

Zhang W, Qiu J, Feng H, Zang L, Sakai E. Increase in stability of cellulase immobilized on functionalized magnetic nanospheres. J Magn Mater. 2015;375:117–23.

Mubarak NM, Wong JR, Tan KW, Sahu JN, Abdullah EC, Jayakumar NS, et al. Immobilization of cellulase enzyme on functionalized multiwall carbon nanotubes. J Mol Catal B Enzym. 2014;107:124–31.

Mishra A, Sardar M. Cellulase assisted synthesis of nano-silver and gold: application as immobilization matrix for biocatalysis. Int J Biol Macromol. 2015;7:105– 13.

Percival Zhang YH, Himmel ME, Mielenz JR. Outlook for cellulase improvement: screening and selection strategies. Biotechnol Adv. 2006;24(5):452–81.

Zhang D, Hegab HE, Lvov Y, Snow LD, Palmer J. Immobilization of cellulase on a silica gel substrate modified using a 3 APTES self assembled monolayer. SpringerPlus. 2016. DOI: 10.1186/s40064-016-1682-y.

Taha ASJ, Taha AJ, Faisal ZG. Purification and Kinetic Study on Cellulase Produced by Local Trichoderma viride. IJACEBS. 2014;1(2):172-5.

Kovalev T. A Physical-chemical and kinetic-thermodynamic aspects of catalysis free and immobilized amylase. Dis Dr biol Sciences. 1998.

Mandels M, Andreotii RC. Measurement of saccharifying Cellulase. Biotechnol Bioeng Symp. 1976;6:21-3.

Woodward J. Immobilized cellulases for cellulose utilization. J Biotechnol. 1989;11:299-311.

Yoshimoto M, Li C, Matsunaga T, et al. Biotechnol Prog. 2006;22:459-64.

Wu L, Yuan X, Sheng J. J Memb Sci. 2005;250:167-73.

Sinegani AAS, Emtiazi G, Shariatmadari H. J Colloid Interface Sci. 2005;290:39-44.

Hideno A, Ogbonna JC, Aoyagi H, Tanaka H. Acetylation of loofa (Luffa cylindrica) sponge as immobilization carrier for bioprocesses involving cellulose. J Biosci Bioeng. 2007;103(4):311-7.

Chandra MS, Viswanath B, Rajasekhar Reddy B. Cellulolytic enzymes on lignocellulosic substrates in solid state fermentation by Aspergillus niger. Ind J Microbiol. 2007;47(4):323-8.

Daoud FB, Kaddour S, Sadoun T. Colloids and Surfaces B: Biointerfaces 2010;75:93-9.

Taha ASJ. Investigation for the alteration in some kinetics parameters of free and immobilized cellulase from local fungus Trichoderma viride.DJPS. 2016;12 (4):126-31.

Zelenkov VN. Substance on the basis of various forms of dry Jerusalem artichoke a promising basis for the development of functional medical products preventative VN Zelenkov / Unconventional natural resources, innovative technologies and Products: Fri. Scientific. tr. - Moscow: Publishing House of the Academy of Natural Sciences, Maano; 2001: 73-78.

DOI: http://dx.doi.org/10.26510/2394-0859.pbe.2017.02


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