Lipase Immobilization by Adsorption Techniques on The Hydrophobically Modified Matrix: A Review
|International Journal of Engineering Trends and Technology (IJETT)||
|© 2021 by IJETT Journal|
|Year of Publication : 2021|
|Authors : Edy Subroto, Siti Nurhasanah, S.Joni Munarso
|DOI : 10.14445/22315381/IJETT-V69I1P208|
MLA Style: Edy Subroto, Siti Nurhasanah, S.Joni Munarso "Lipase Immobilization by Adsorption Techniques on The Hydrophobically Modified Matrix: A Review" International Journal of Engineering Trends and Technology 69.1(2021):49-55.
APA Style:Edy Subroto, Siti Nurhasanah, S.Joni Munarso. Lipase Immobilization by Adsorption Techniques on The Hydrophobically Modified Matrix: A Review International Journal of Engineering Trends and Technology, 69(1), 49-55.
Lipase immobilization has been carried out by various methods, each of which has various advantages. One of the rapidly developing lipase immobilization techniques is the adsorption method. This review describes the immobilization of lipase with adsorption techniques, especially about the use of various types of matrices and matrix surface modification techniques that can improve the lipase microenvironment. The adsorption method has several advantages over other ways, including easy preparation, the low cost can be regenerated, and the matrix`s surface can be modified to improve lipase activity and stability. Hydrophobic modification of the surface matrix can encourage the lid lipase to open easily, thereby increasing its activity. Adsorption immobilized lipases have also been shown to be effective and stable over several applications for various reactions. However, the challenge in the hydrophobic modification is that the loading of lipase protein is generally relatively lower than that of the hydrophilic matrix. Therefore, further, development is needed by utilizing various types of matrices, hydrophobic groups, lipases, and modification techniques to increase their loading capacity, activity, and stability.
 P. K. Robinson, Enzymes: principles and biotechnological applications, Essays Biochem.,59 (2015) 1–41.
 S. Liang, X.-L. Wu, J. Xiong, M.-H. Zong, and W.-Y. Lou, Metal-organic frameworks as novel matrices for efficient enzyme immobilization: An updated review, Coord. Chem. Rev.,406(2020) 213149.
 D.-M. Liu and C. Dong, Recent advances in nano-carrier immobilized enzymes and their applications, Process Biochem.,92(2020) 464–475.
 D. Pandey, A. Daverey, and K. Arunachalam, Biochar: Production, properties and emerging role as a support for enzyme immobilization, J. Clean. Prod., 255(2020) 120267.
 J. Zdarta, A. S. Meyer, T. Jesionowski, and M. Pinelo, A general overview of support materials for enzyme immobilization: Characteristics, properties, practical utility, Catalysts, 8(2)(2018).
 A. Zare, A.-K. Bordbar, F. Jafarian, and S. Tangestaninejad, Candida rugosa lipase immobilization on various chemically modified Chromium terephthalate MIL-101, J. Mol. Liq.,254(2018) 137–144.
 D. K. Bedade, Y. B. Sutar, and R. S. Singhal, Chitosan coated calcium alginate beads for covalent immobilization of acrylamidase: Process parameters and removal of acrylamide from coffee, Food Chem., 275(2019) 95–104.
 P. Chandra, Enespa, R. Singh, and P. K. Arora, Microbial lipases and their industrial applications: a comprehensive review, Microb. Cell Fact.,19(1)(2020) 169.
 E. Subroto, Supriyanto, T. Utami, and C. Hidayat, Enzymatic glycerolysis–interesterification of palm stearin–olein blend for synthesis structured lipid containing high mono- and diacylglycerol, Food Sci. Biotechnol., 28(2)(2019) 511–517.
 A. Mehta, U. Bodh, and R. Gupta, Fungal lipases: A review, J. Biotech Res., 8(1)(2017) 58–77.
 B. Thangaraj and P. R. Solomon, Immobilization of Lipases – A Review. Part I: Enzyme Immobilization, ChemBioEng Rev., 6(5)(2019) 157–166.
 E. Subroto, Monoacylglycerols and diacylglycerols for fat-based food products: a review, Food Res., 4(4) (2020) 932–943.
 A. Houde, A. Kademi, and D. Leblanc, Lipases and their industrial applications, Appl. Biochem. Biotechnol., 118(1)(2004) 155–170.
 E. Subroto, R. Indiarto, A. D. Pangawikan, S. Huda, and V. P. Yarlina, Characteristics, immobilization, and Candida application rugosa lipase: a review, Food Res.,4(5)(2020) 1391–1401.
 T. O. Akanbi, A. J. Sinclair, and C. J. Barrow, Pancreatic lipase selectively hydrolyses DPA over EPA and DHA due to double bonds in the fatty acid rather than regioselectivity, Food Chem.,160 (2014) 61–66.
 E. Subroto, R. Indiarto, M. Djali, and H. D. Rosyida, Production and Application of Crosslinking- Modified Starch as Fat Replacer : A Review, Int. J. Eng. Trends Technol., 68(12)(2020) 26–30.
 B. H. Kim and C. C. Akoh, Recent Research Trends on the Enzymatic Synthesis of Structured Lipids, J. Food Sci., 80(8)(2015) 1713–1724.
 Q. D. Utama, A. B. Sitanggang, D. R. Adawiyah, and P. Hariyadi, Lipase-Catalyzed Interesterification for the Synthesis of Medium-Long-Medium (MLM) Structured Lipids - A Review, Food Technol. Biotechnol.,57(3)305–318,(2019).
 F. J. Contesini, M. G. Davanço, G. P. Borin, K. G. Vanegas, G. Cirino, and R. R. De Melo, Advances in Recombinant Lipases : Application in the Pharmaceutical Industry, Catalysts, 10(9)(2020) 1032.
 G. Angajala, P. Pavan, and R. Subashini, Lipases: An overview of its current challenges and prospectives in the revolution of biocatalysis, Biocatal. Agric. Biotechnol., 7(2016) 257–270.
 S. Ali, W. Zafar, S. Shafiq, and M. Manzoor, Enzymes Immobilization: An Overview Of Techniques, Support Materials And Its Applications, Int. J. Sci. Technol. Res.,6(7)(2017) 64–72.
 W. Shuai, R. K. Das, M. Naghdi, S. K. Brar, and M. Verma, A Review on the Important Aspects of Lipase Immobilization Nanomaterials, Laryngoscope,(2014) 2–31.
 A. Idris and A. Bukhari, Immobilized Candida antarctica lipase B: Hydration, stripping off and application in ring-opening polyester synthesis, Biotechnol. Adv.,30(3) (2012) 550–563.
 H. H. Nguyen and M. Kim, An Overview of Techniques in Enzyme Immobilization, Appl. Sci. Converg. Technol.,26(6)(2017) 157–163.
 F. B. H. Rehm, S. Chen, and B. H. A. Rehm, Enzyme Engineering for In Situ Immobilization, Molecules,21(10)(2016) 1370.
 S. Datta, L. R. Christena, and Y. R. S. Rajaram, Enzyme immobilization: an overview on techniques and support materials,3 Biotech, 3(2013) 1–9.
 M. Bilal and H. M. N. Iqbal, Naturally-derived biopolymers: Potential platforms for enzyme immobilization, Int. J. Biol. Macromol., 130, 462–482, 2019.
 X. Xiang, H. Suo, C. Xu, and Y. Hu, "Covalent immobilization of lipase onto chitosan-mesoporous silica hybrid nanomaterials by carboxyl functionalized ionic liquids as the coupling agent, Colloids Surfaces B Biointerfaces,165,262–269 (2018).
 M. Bilal and H. M. N. Iqbal, Sustainable bioconversion of food waste into high-value products by immobilized enzymes to meet bio-economy challenges and opportunities – A review, Food Res. Int.,123(2019) 226–240.
 M. J. Moehlenbrock and S. D. Minteer, Introduction to the Field of Enzyme Immobilization and Stabilization, in Enzyme Stabilization and Immobilization, S. Minteer, Ed. New York: Humana Press, (2017) 1–7.
 M. Bilal, M. Asgher, H. Cheng, Y. Yan, and H. M. N. Iqbal, "Multi-point enzyme immobilization, surface chemistry, and novel platforms: a paradigm shift in biocatalyst design, Crit. Rev. Biotechnol., 39(2)(2019) 202–219.
 J. C. S. dos Santos, O. Barbosa, C. Ortiz, A. Berenguer-Murcia, R. C. Rodrigues, and R. Fernandez-Lafuente, "Importance of the Support Properties for Immobilization or Purification of Enzymes, ChemCatChem, 7(2015) 2413–2432.
 M. C. P. Gonçalves, T. G. Kieckbusch, R. F. Perna, J. T. Fujimoto, S. A. V. Morales, and J. P. Romanelli, "Trends on enzyme immobilization researches based on bibliometric analysis, Process Biochem., (2018)1–16.
 C. Cai, Y. Gao, Y. Liu, N. Zhong, and N. Liu, "Immobilization of Candida antarctica lipase B onto SBA-15 and their application in glycerolysis for diacylglycerols synthesis, Food Chem.,212,205–212.
 N. R. Mohamad, N. H. C. Marzuki, N. A. Buang, F. Huyop, and R. A. Wahab, An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes, Biotechnol. Biotechnol. Equip., 29(2)(2016) 205–220, 2015.
 A. A. Homaei, R. Sariri, F. Vianello, and R. Stevanato, Enzyme immobilization: an update, J. Chem. Biol., 6(4)(2013) 185–205.
 S. Gao, Y. Wang, T. Wang, G. Luo, and Y. Dai, Immobilization of lipase on methyl-modified silica aerogels by physical Adsorption, Bioresour. Technol., 100(2)(2009) 996–999.
 H. Dong, J. Li, Y. Li, L. Hu, and D. Luo, Improvement of catalytic activity and lipase stability by immobilization on organobentonite, Chem. Eng. J., 181–182(2012) 590–596.
 T. Jesionowski, J. Zdarta, and B. Krajewska, Enzyme immobilization by Adsorption: a review, Adsorption, 20(5)(2014) 801–821.
 E. A. Manoel, J. C. S. dos Santos, D. M. G. Freire, N. Rueda, and R. Fernandez-Lafuente, Immobilization of lipases on hydrophobic supports involves the open form of the enzyme, Enzyme Microb. Technol.,71(2015) 53–57,
 H. Hilmanto, C. Hidayat, and P. Hastuti, Surface Modification of Macroporous Matrix for Immobilization of Lipase for Fructose Oleic Ester Synthesis, Bull. Chem. React. Eng. Catal., 11(3)(2016) 339–345.
 E. Subroto, M. F. Wisamputri, Supriyanto, T. Utami, and C. Hidayat, Enzymatic and chemical synthesis of high mono diacylglycerol from palm stearin and olein blend at a different type of reactor stirrers, J. Saudi Soc. Agric. Sci.,19(1)(2020) 31–36.
 B. Chen, C. Yin, Y. Cheng, W. Li, Z. A. Cao, and T. Tan, "Using silk is woven fabric as support for lipase immobilization: The effect of surface hydrophilicity/hydrophobicity on enzymatic activity and stability, Biomass and Bioenergy,39(2012) 59–66.
 M. Yigitoglu and Z. Temoçin, Immobilization of Candida rugosa lipase on glutaraldehyde-activated polyester fiber and its application for hydrolysis of some vegetable oils, J. Mol. Catal. B Enzym.,66(2010) 1–2,130–135.
 J. J. Bassi et al., Interfacial activation of lipases on hydrophobic support and application in synthesizing a lubricant ester, Int. J. Biol. Macromol.,92,(2016)900–909.
 L. Amirkhani, J. Moghaddas, and H. Jafarizadeh-Malmiri, Optimization of Candida rugosa Lipase Immobilization Parameters on Magnetic Silica Aerogel Using Adsorption Method, Iran. J. Chem. Eng.,13(3) (2016) 19–31.
 M. Nasratun et al., Immobilization of Lipase from Candida rugosa on Chitosan Beads for Transesterification Reaction, Journal of Applied Sciences, 21(10)(2010) 2701–2704.
 B. S. Kaja, S. Lumor, S. Besong, B. Taylor, and G. Ozbay, Investigating Enzyme Activity of Immobilized Candida rugosa Lipase, J. Food Qual.,(2018).
 M. Cea, M. E. González, M. Abarzúa, and R. Navia, Enzymatic esterification of oleic acid by Candida rugosa lipase immobilized onto biochar,J. Environ. Manage.,242(2018) 171–177.
 B. Öztürk, Immobilization of Lipase from Candida rugosa on Hydrophobic and Hydrophilic Supports, ?zmir Institute of Technology, Turkey, (2001).
 P. Sabuquillo, J. Reina, G. Fernandez-Lorente, J. M. Guisan, and R. Fernandez-Lafuente, Interfacial affinity chromatography` of lipases: Separation of different fractions by selective Adsorption on supports activated with hydrophobic groups, Biochim. Biophys. Acta - Protein Struct. Mol. Enzymol., 1388(2)(1998) 337–348.
 P. Reis, K. Holmberg, H. Watzke, M. Leser, and R. Miller, Lipases at interfaces: A review, Adv. Colloid Interface Sci.,147–148,(2009) 237–250
 Chernet Merkneh, Mulugeta Tadesse, Mihiretu Gezahagn, Development and Property Exploration of Composite Structural Insulated Panel as Alternative House Construction Material, IJETT International Journal of Mechanical Engineering, 7.6 (2020): 1-12.
Immobilization, lipase, Adsorption, hydrophobic modification.