Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry
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2016
Authors
Trbojević-Ivić, JovanaVeličković, Dušan
Dimitrijević, Aleksandra
Bezbradica, Dejan
Dragacevic, Vladimir
Gavrović-Jankulović, Marija
Milosavić, Nenad
Article (Published version)
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BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the... prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry
Keywords:
Candida rugosa lipase / immobilization / hydroxyapatite / organic solvents / methyl acetateSource:
Journal of the Science of Food and Agriculture, 2016, 96, 12, 4281-4287Publisher:
- Wiley-Blackwell, Hoboken
Funding / projects:
- Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-MESTD-Basic Research (BR or ON)-172049)
- Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
DOI: 10.1002/jsfa.7641
ISSN: 0022-5142
PubMed: 26801832
WoS: 000380729800040
Scopus: 2-s2.0-84979295840
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Trbojević-Ivić, Jovana AU - Veličković, Dušan AU - Dimitrijević, Aleksandra AU - Bezbradica, Dejan AU - Dragacevic, Vladimir AU - Gavrović-Jankulović, Marija AU - Milosavić, Nenad PY - 2016 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1943 AB - BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry PB - Wiley-Blackwell, Hoboken T2 - Journal of the Science of Food and Agriculture T1 - Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry VL - 96 IS - 12 SP - 4281 EP - 4287 DO - 10.1002/jsfa.7641 ER -
@article{ author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Bezbradica, Dejan and Dragacevic, Vladimir and Gavrović-Jankulović, Marija and Milosavić, Nenad", year = "2016", abstract = "BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry", publisher = "Wiley-Blackwell, Hoboken", journal = "Journal of the Science of Food and Agriculture", title = "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry", volume = "96", number = "12", pages = "4281-4287", doi = "10.1002/jsfa.7641" }
Trbojević-Ivić, J., Veličković, D., Dimitrijević, A., Bezbradica, D., Dragacevic, V., Gavrović-Jankulović, M.,& Milosavić, N.. (2016). Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. in Journal of the Science of Food and Agriculture Wiley-Blackwell, Hoboken., 96(12), 4281-4287. https://doi.org/10.1002/jsfa.7641
Trbojević-Ivić J, Veličković D, Dimitrijević A, Bezbradica D, Dragacevic V, Gavrović-Jankulović M, Milosavić N. Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. in Journal of the Science of Food and Agriculture. 2016;96(12):4281-4287. doi:10.1002/jsfa.7641 .
Trbojević-Ivić, Jovana, Veličković, Dušan, Dimitrijević, Aleksandra, Bezbradica, Dejan, Dragacevic, Vladimir, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry" in Journal of the Science of Food and Agriculture, 96, no. 12 (2016):4281-4287, https://doi.org/10.1002/jsfa.7641 . .