Abstract
Lipase is a lipolytic enzyme that catalyzes the hydrolysis of lipids and esterification reactions. Lipase has been utilized in industrial uses, food processing, and therapeutic applications as a biocatalyst. However, substrates of lipase are often insoluble in water, and this problem limits its utility. Lipases are also used in organic solvents where the solvent-stability of lipase is an important factor. There is a huge number of approaches that can be undertaken to improve the organic solvent-stability of lipases. For example, screening of solvent-tolerant lipase in nature and direct evolution of lipase using genetic engineering are some of the employed approaches. Here, we focus on approaches based on the chemical treatment of lipases for modification and immobilization. The solvent-stability of lipase was improved by the attachment of other molecules, such as surfactants, polymers, and carbohydrates. The immobilization of the enzyme is been known to be an effective approach for not only recycling the enzyme but also its stabilization. Several reports have demonstrated that the solvent-stability of lipase is also improved by immobilization. In this review, we provide an overview of the approaches used to improve the solvent-stability of lipase.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Barbosa O, Ortiz C, Berenguer-Murcia Á, Torres R, Rodrigues RC, Fernandez-Lafuente R (2014) Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization. RSC Adv 4:1583–1600. https://doi.org/10.1039/C3RA45991H
Basri M, Ampon K, Yunus WMZW, Razak CNA, Salleh AB (1995) Synthesis of fatty esters by polyethylene glycol-modified lipase. J Chem Technol Biotechnol 64:10–16. https://doi.org/10.1002/jctb.280640103
Bastida A, Sabuquillo P, Armisen P, Fernandez-Lafuente R, Huguet J, Guisan JM (1998) A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol Bioeng 58:486–493. https://doi.org/10.1002/(SICI)1097-0290(19980605)58:5%3c486:AID-BIT4%3e3.0.CO;2-9
Boutureira and Bernardes (2015) Boutureira O and Bernardes GJ (2015) Advances in chemical protein modification. Chem Rev 115:2174–2195. https://doi.org/10.1021/cr500399p
Carvalho CM, Cabral JM (2000) Reverse micelles as reaction media for lipases. Biochimie 82:1063–1085. https://doi.org/10.1016/S0300-9084(00)01187-1
Desai PD, Dave AM, Devi S (2006) Alcoholysis of salicornia oil using free and covalently bound lipase onto chitosan beads. Food Chem 95:193–199. https://doi.org/10.1016/j.foodchem.2004.12.030
Díaz-Rodríguez A, Davis BG (2011) Chemical modification in the creation of novel biocatalysts. Curr Opin Chem Biol 15:211–219. https://doi.org/10.1016/S0958-1669(03)00098-3
Doukyu N, Ogino H (2010) Organic solvent-tolerant enzymes. Biochem Eng J 48:270–282. https://doi.org/10.1016/j.bej.2009.09.009
Fang Y, Lu Z, Lv F, Bie X, Liu S, Ding Z, Xu W (2006) A newly isolated organic solvent tolerant Staphylococcus saprophyticus M36 produced organic solvent-stable lipase. Curr Microbiol 53:510–515. https://doi.org/10.1007/s00284-006-0260-x
Foresti ML, Ferreira ML (2007) Chitosan-immobilized lipases for the catalysis of fatty acid esterifications. Enzyme Microb Technol 40:769–777. https://doi.org/10.1016/j.enzmictec.2006.06.009
Gao S, Wang Y, Diao X, Luo G, Dai Y (2010) Effect of pore diameter and cross-linking method on the immobilization efficiency of Candida rugosa lipase in SBA-15. Bioresour Technol 101:3830–3837. https://doi.org/10.1016/j.biortech.2010.01.023
Guncheva MH, Zhiryakova D (2008) High-yield synthesis of wax esters catalysed by modified Candida rugosa lipase. Biotechnol Lett 30:509–512. https://doi.org/10.1007/s10529-007-9554-8
Hama S, Yoshida A, Nakashima K, Noda H, Fukuda H, Kondo A (2010) Surfactant-modified yeast whole-cell biocatalyst displaying lipase on cell surface for enzymatic production of structured lipids in organic media. Appl Microbiol Biotechnol 87:537–543. https://doi.org/10.1007/s00253-010-2519-1
Hanefeld U, Gardossi L, Magner E (2009) Understanding enzyme immobilisation. Chem Soc Rev 38:453–468. https://doi.org/10.1039/b711564b
Hasan F, Shah AA, Hameed A (2006) Industrial applications of microbial lipases. Enzyme Microb Technol 39:235–251. https://doi.org/10.1016/j.enzmictec.2005.10.016
Heater BS, Lee MM, Chan MK (2018) Direct production of a genetically-encoded immobilized biodiesel catalyst. Sci Rep 8:12783. https://doi.org/10.1038/s41598-018-31213-y
Heater BS, Chan WS, Lee MM, Chan MK et al (2019) Directed evolution of a genetically encoded immobilized lipase for the efficient production of biodiesel from waste cooking oil. Biotechnol Biofuels 12:165. https://doi.org/10.1186/s13068-019-1509-5
Hun CJ, Rahman RNZA, Salleh AB, Basri M (2003) A newly isolated organic solvent tolerant Bacillus sphaericus 205y producing organic solvent-stable lipase. Biochem Eng J 15:147–151. https://doi.org/10.1016/S1369-703X(02)00185-7
Hung TC, Giridhar R, Chiou SH, Wu WT (2003) Binary immobilization of Candida rugosa lipase on chitosan. J Mol Catal B 26:69–78. https://doi.org/10.1016/S1381-1177(03)00167-X
Inada Y, Takahashi K, Yoshimoto T, Ajima A, Matsushima A, Saito Y (1986) Application of polyethylene glycol-modified enzymes in biotechnological processes: organic solvent-soluble enzymes. Trends Biotechnol 4:190–194. https://doi.org/10.1016/0167-7799(86)90244-1
Ito Y, Fujii H, Imanishi Y (1994) Modification of lipase with various synthetic polymers and their catalytic activities in organic solvent. Blotechnol Prog 10:398–402. https://doi.org/10.1021/bp00028a009
Iyer PV, Ananthanarayan L (2008) Enzyme stability and stabilization—aqueous and non-aqueous environment. Proc Biochem 43:1019–1032. https://doi.org/10.1016/j.procbio.2008.06.004
Jesionowski T, Zdarta J, Krajewska B (2014) Enzyme immobilization by adsorption: a review. Adsorption 20:801–821. https://doi.org/10.1007/s10450-014-9623-y
Kajiwara S, Komatsu K, Yamada R, Matsumoto T, Yasuda M, Ogino H (2019a) Improvement of the organic solvent stability of a commercial lipase by chemical modification with dextran. Biochem Eng J 142:1–6. https://doi.org/10.1016/j.bej.2018.11.003
Kajiwara S, Komatsu K, Yamada R, Matsumoto T, Yasuda M, Ogino H (2019b) Modification of lipase from Candida cylindracea with dextran using the borane-pyridine complex to improve organic solvent stability. J Biotechnol 296:1–6. https://doi.org/10.1016/j.jbiotec.2019.02.009
Kartal F, Janssen MH, Hollmann F, Sheldon RA, Kılınc A (2011) Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as cross-linked enzyme aggregates (CLEAs). J Mol Catal B 71:85–89. https://doi.org/10.1016/j.molcatb.2011.04.002
Khalaf N, Govardhan CP, Lalonde JJ, Persichetti RA, Wang YF, Margolin AL (1996) Cross-linked enzyme crystals as highly active catalysts in organic solvents. J Am Chem Soc 118:5494–5495. https://doi.org/10.1021/ja960081s
Kreiner M, Moore BD, Parker MC (2001) Enzyme-coated micro-crystals: a 1-step method for high activity biocatalyst preparation. Chem Commun 12:1096–1097. https://doi.org/10.1039/B100722J
Kumar A, Dhar K, Kanwar SS, Arora PK (2016) Lipase catalysis in organic solvents: advantages and applications. Biol Proced Online 18:2. https://doi.org/10.1186/s12575-016-0033-2
Lalonde JJ, Govardhan C, Khalaf N, Martinez AG, Visuri K, Margolin AL (1995) Cross-linked crystals of Candida rugosa lipase: highly efficient catalysts for the resolution of chiral esters. J Am Chem Soc 117:6845–6852. https://doi.org/10.1021/ja00131a006
Lee JK, Kim MJ (2002) Ionic liquid-coated enzyme for biocatalysis in organic solvent. J Org Chem 67:6845–6847. https://doi.org/10.1021/jo026116q
Mogi K, Nakajima M, Mukataka S (1999) Surfactant modification of lipases for lipid interesterification and hydrolysis reactions. J Am Oil Chem Soc 76:1259–1264. https://doi.org/10.1007/s11746-999-0136-x
Murakami M, Kawasaki Y, Kawanari M, Okai H (1993) Transesterification of oil by fatty acid-modified lipase. J Am Oil Chem Soc 70:571–574. https://doi.org/10.1007/BF02545321
Mutschler J, Rausis T, Bourgeois JM, Bastian C, Zufferey D, Mohrenz IV, Fischer F (2009) Ionic liquid-coated immobilized lipase for the synthesis of methylglucose fatty acid esters. Green Chem 11:1793–1800. https://doi.org/10.1039/B916016G
Nishio T, Takahashi K, Yoshimoto T, Kodera Y, Saito Y, Inada Y (1987) Terpene alcohol ester synthesis by polyethylene glycol-modified lipase in benzene. Biotechnol Lett 9:187–190. https://doi.org/10.1007/BF01024562
Ogino H, Ishikawa H (2001) Enzymes which are stable in the presence of organic solvents. J Biosci Bioeng 91:109–116. https://doi.org/10.1016/S1389-1723(01)80051-7
Ogino H, Nakagawa S, Shinya K, Muto T, Fujimura N, Yasuda M, Ishikawa H (2000) Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03. J Biosci Bioeng 89:451–457. https://doi.org/10.1016/S1389-1723(00)89095-7
Okahata Y, Ijiro K (1988) A lipid-coated lipase as a new catalyst for triglyceride synthesis in organic solvents. J Chem Soc Chem Commun. https://doi.org/10.1039/C39880001392
Okahata Y, Hatano A, Ijiro K (1995) Enhancing enantioselectivity of a lipid-coated lipase via imprinting methods for esterification in organic solvents. Tetrah Asym 6:1311–1322. https://doi.org/10.1016/0957-4166(95)00165-L
Persson M, Mladenoska I, Wehtje E, Adlercreutz P (2002) Preparation of lipases for use in organic solvents. Enzyme Microb Technol 31:833–841. https://doi.org/10.1016/S0141-0229(02)00184-9
Priyanka P, Tan Y, Kinsella GK, Henehan GT, Ryan BJ (2019) Solvent stable microbial lipases: current understanding and biotechnological applications. Biotechnol Lett 41:203–220. https://doi.org/10.1007/s10529-018-02633-7
Rodrigues ÁR, Cabral JM, Taipa MÂ (2002) Immobilization of Chromobacterium viscosum lipase on Eudragit S-100: coupling, characterization and kinetic application in organic and biphasic media. Enzyme Microb Technol 31:133–141. https://doi.org/10.1016/S0141-0229(02)00087-X
Romero O, de Las RB, Lopez-Tejedor D, Palomo JM (2018) Effect of site-specific peptide-tag labeling on the biocatalytic properties of thermoalkalophilic lipase from geobacillus thermocatenulatus. ChemBioChem 19:369–378. https://doi.org/10.1002/cbic.201700466
Sanchez-Montero JM, Hamon V, Thomas D, Legoy MD (1991) Modulation of lipase hydrolysis and synthesis reactions using carbohydrates. Biochim Biophys Acta 1078:345–350. https://doi.org/10.1016/0167-4838(91)90155-S
Sheldon RA (2011) Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl Microbiol Biotechnol 92:467–477. https://doi.org/10.1007/s00253-011-3554-2
Shuai W, Das RK, Naghdi M, Brar SK, Verma M (2017) A review on the important aspects of lipase immobilization on nanomaterials. Biotechnol Appl Biochem 64:496–508. https://doi.org/10.1002/bab.1515
Singh RK, Tiwari MK, Singh R, Lee JK (2013) From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes. Int J Mol Sci 14:1232–1277. https://doi.org/10.3390/ijms14011232
Stamatis H, Xenakis A, Kolisis FN (1999) Bioorganic reactions in microemulsions: the case of lipases. Biotechnol Adv 17:293–318. https://doi.org/10.1016/S0734-9750(99)00007-5
Takahashi K, Nishimura H, Yoshimoto T, Okada M, Ajima A, Matsushima A, Tamaura Y, Saito Y, Inada Y (1984) Polyethylene glycol-modified enzymes trap water on their surface and exert enzymic activity in organic solvents. Biotechnol Lett 6:765–770. https://doi.org/10.1007/BF00134715
Vaidya A, Miller E, Bohling J, Gross RA (2006a) Immobilization of Candida antarctica lipase B on macroporous resins: effects of resin chemistry, reaction conditions and resin hydrophobicity. Polym Prepr 47:247–248
Vaidya A, Xie W, Gao W, Miller E, Bohling J, Gross RA (2006b) Enzyme immobilization without a support: Candida antaratica lipase B(CALB) self-crosslinked aggregates. Polym Prepr 47:236–237
Vaidya A, Gera G, Ramakrishna S (2008) Evaluation and optimization of immobilized lipase for esterification of fatty acid and monohydric alcohol. World J Microbiol Biotechnol 24:2987–2995. https://doi.org/10.1007/s11274-008-9842-z
Vaidya et al (2019) Vaidya A, Hussain I, Gaugler M, Smith DA (2019). Synthesis of graft copolymers of chitosan-poly(caprolactone) by lipase catalysed reactive extrusion. Carbohydr Polym 217:98–109. https://doi.org/10.1016/j.carbpol.2019.03.081
Villeneuve P, Muderhwa JM, Graille J, Haas MJ (2000) Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J Mol Catal B 9:113–148. https://doi.org/10.1016/S1381-1177(99)00107-1
Wu Y, Wang Y, Luo G, Dai Y (2009) In situ preparation of magnetic Fe3O4-chitosan nanoparticles for lipase immobilization by cross-linking and oxidation in aqueous solution. Bioresour Technol 100:3459–3464. https://doi.org/10.1016/j.biortech.2009.02.018
Xie W, Huang M (2018) Immobilization of Candida rugosa lipase onto graphene oxide Fe3O4 nanocomposite: Characterization and application for biodiesel production. Energy Convers Manag 159:42–53. https://doi.org/10.1016/j.enconman.2018.01.021
Yan J, Yan Y, Liu S, Hu J, Wang G (2011) Preparation of cross-linked lipase-coated micro-crystals for biodiesel production from waste cooking oil. Bioresour Technol 102:4755–4758. https://doi.org/10.1016/j.biortech.2011.01.006
Zaks A, Klibanov AM (1984) Enzymatic catalysis in organic media at 100°C. Science 2:1249–1251. https://doi.org/10.1126/science.6729453
Zheng J, Xu L, Liu Y, Zhang X, Yan Y (2012) Lipase-coated K2SO4 micro-crystals: preparation, characterization, and application in biodiesel production using various oil feedstocks. Bioresour Technol 110:224–231. https://doi.org/10.1016/j.biortech.2012.01.088
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interests.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Matsumoto, T., Yamada, R. & Ogino, H. Chemical treatments for modification and immobilization to improve the solvent-stability of lipase. World J Microbiol Biotechnol 35, 193 (2019). https://doi.org/10.1007/s11274-019-2777-8
Received:
Accepted:
Published:
DOI: https://doi.org/10.1007/s11274-019-2777-8