CHARACTERIZATION OF PREDICTED BACTERIAL COLD-ADAPTED LIPASE FROM SEAFOOD COLD STORAGE
Keywords:Bacteria, Cold-Adapted Lipase, Characterization, Fish Cold Storage
Lipases constitute as top three most important group of enzymes along with carbohydrases and proteases, and are widely used in various industries. In particular, lipase that perform high activity at low temperatures, or referred as cold adapted lipase (CLPs) considered as attractive catalyst due to its activity at low temperature. This unique feature is the main advantage of cold adapted lipase utilization because it requires a low energy source that is correlated with lower production costs and energy. In addition, reactions occur in cold temperatures may result in better product quality. The purpose of this research was to perform screening and characterization of bacterial cold adapted lipase from seafood cold storage. Among 53 isolates, Kr_16_30, TI_37_14 and Kr_16_28 showed the highest activity with 4.12 U/mL; 3.87 U/mL and 3.21 U/mL, respectively. Isolates Kr_16_30 seemed to be typical cold adapted lipase with optimum temperature at 20°C and pH 7. Isolates Kr_16_28 performed highest lipolytic activity at 30°C while TI_37_14 suspected to be similar to typical mesophilic lipase with optimum temperature at 40°C. Species identification based on 16s rRDA sequencing revealed that isolates Kr_16 30 and Kr_16 28 are belong to genus Pseudomonas and Bacillus, repectively.
Collins, T., Gerday, C., & Meuwis, M. (2012) Cold-Adapted Enzymes.
Cowan, D. (2010) Concentration of Omega-3 Fatty Acids Using Enzymes. Agro FOOD industry hi-tech,
Dieckelmann, M., Johnson, L. A., & Beacham, I. R. (1998) The diversity of lipases from psychrotrophic strains of pseudomonas : A novel lipase from a highly lipolytic strain of Pseudomonas fluorescens, Journal of Applied Microbiology, Vol. 85, No. 3, 527-536. Retrieved from https://doi.org/10.1046/j.1365-2672.1998.853530.x DOI: https://doi.org/10.1046/j.1365-2672.1998.853530.x
Domínguez De María, P., Carboni-Oerlemans, C., Tuin, B., Bargeman, G., Van Der Meer, A., & Van Gemert, R. (2005) Biotechnological applications of Candida antarctica lipase A : State-of-the-art, Journal of Molecular Catalysis B : Enzymatic, Vol. 37, No. 1-6, 36-46. Retrieved from https://doi.org/10.1016/j.molcatb.2005.09.001 DOI: https://doi.org/10.1016/j.molcatb.2005.09.001
Feller, G. (2010) Protein stability and enzyme activity at extreme biological temperatures, Journal of Physics Condensed Matter, Vol. 22, No. 32, 1-17. Retrieved from https://doi.org/10.1088/0953-8984/22/32/323101 DOI: https://doi.org/10.1088/0953-8984/22/32/323101
Feller, G., Thiry, M., Arpigny, J. L., & Gerday, C. (1991) Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic antarctic strain Moraxella TA144. Gene, Vol. 102, No. 1, 111-115. Retrieved from https://doi.org/10.1016/0378-1119(91)90548-P DOI: https://doi.org/10.1016/0378-1119(91)90548-P
Georlette, D., Blaise, V., Collins, T., D'Amico, S., Gratia, E., Hoyoux, A., Marx, J. C., Sonan, G., Feller, G., & Gerday, C. (2004) Some like it cold : Biocatalysis at low temperatures, FEMS Microbiology Reviews, Vol. 28, No. 1, 25-42. Retrieved from https://doi.org/10.1016/j.femsre.2003.07.003 DOI: https://doi.org/10.1016/j.femsre.2003.07.003
Gupta, R., Gupta, N., & Rathi, P. (2004) Bacterial lipases : An overview of production, purification and biochemical properties, Applied Microbiology and Biotechnology, Vol. 64, No. 6, 763-781. Retrieved from https://doi.org/10.1007/s00253-004-1568-8 DOI: https://doi.org/10.1007/s00253-004-1568-8
Jaeger, K. E., & Eggert, T. (2002) Lipases for biotechnology, Current Opinion in Biotechnology, Vol. 13, No. 4, 390-397. Retrieved from https://doi.org/10.1016/S0958-1669(02)00341-5 DOI: https://doi.org/10.1016/S0958-1669(02)00341-5
Joseph, B., Ramteke, P. W., & Thomas, G. (2008) Cold active microbial lipases : Some hot issues and recent developments. Biotechnology Advances, Vol. 26, No. 5, 457-470. Retrieved from https://doi.org/10.1016/j.biotechadv.2008.05.003 DOI: https://doi.org/10.1016/j.biotechadv.2008.05.003
Kavitha, M. (2016) Cold active lipases - an update, Frontiers in Life Science, Vol. 9, No.3, 226-238. Retrieved from https://doi.org/10.1080/21553769.2016.1209134 DOI: https://doi.org/10.1080/21553769.2016.1209134
Kavitha, M., & Shanthi, C. (2013) Isolation and Characterization of Cold active lipase producing Pseudomonas sp. 4 from Marine samples of Tamilnadu Coast, Research Journal of Biotechnology, Vol. 8, No. 4, 4-10.
Kuddus, M., & Ramteke, P. W. (2008) Purification and properties of cold-active metalloprotease from Curtobacterium luteum and effect of culture conditions on production, Shengwu Gongcheng Xuebao/Chinese Journal of Biotechnology, Vol. 24, No. 12, 2074-2080. Retrieved from https://www.sciencedirect.com/science/article/abs/pii/S1872207509600121
Kulakova, L., Galkin, A., Nakayama, T., Nishino, T., & Esaki, N. (2004) Cold-active esterase from Psychrobacter sp. Ant300 : Gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability, Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1696, No. 1, 59-65. Retrieved from https://doi.org/10.1016/j.bbapap.2003.09.008 DOI: https://doi.org/10.1016/j.bbapap.2003.09.008
Mukesh, K., Rejitha, R., Devika, S., Balakumaran, M. D., Rebecca, I. N., & Kalaichelvan, P. T. (2012) Production, optimization and purification of lipase from Bacillus sp. MPTK 912 isolated from oil mill effluent, Advances in Applied Science Research, Vol. 3, No. 2, 930-938.
Rai, B., Shrestha, A., Sharma, S., & Joshi, J. (2014) Screening, Optimization and Process Scale up for Pilot Scale Production of Lipase by Aspergillus niger, Biomedicine and Biotechnology, Vol. 2, No. 3, 54-59. Retrieved from https://doi.org/10.12691/bb-2-3-3
Santiago, M., Ramírez-Sarmiento, C. A., Zamora, R. A., & Parra, L. P. (2016) Discovery, molecular mechanisms, and industrial applications of cold-active enzymes, Frontiers in Microbiology, 7, 1408. Retrieved from https://doi.org/10.3389/fmicb.2016.01408 DOI: https://doi.org/10.3389/fmicb.2016.01408
Xuezheng, L., Shuoshuo, C., Guoying, X., Shuai, W., Ning, D., & Jihong, S. (2010) Cloning and heterologous expression of two cold-active lipases from the Antarctic bacterium Psychrobacter sp. G, Polar Research, Vol. 29, No. 3, 421-429. Retrieved from https://doi.org/10.3402/polar.v29i3.6087 DOI: https://doi.org/10.1111/j.1751-8369.2010.00189.x
Zhang, J. W., & Zeng, R. Y. (2008) Molecular cloning and expression of a cold-adapted lipase gene from an antarctic deep sea psychrotrophic bacterium Pseudomonas sp. 7323, Marine Biotechnology, Vol. 10, No. 5, 2008, 612-621. Retrieved from https://doi.org/10.1007/s10126-008-9099-4 DOI: https://doi.org/10.1007/s10126-008-9099-4
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