The Effect of Calcium Alginate Entrapment on the Stability of Novel Lipases from P. Reinekei and P. brenneri
Trends in Peptide and Protein Sciences,
Vol. 4 (2019),
1 January 2019
,
Page 1-10 (e7)
https://doi.org/10.22037/tpps.v4i0.26682
Abstract
The high cost of soluble enzymes can limit their use for commercial and industrial purposes. Immobilization can enhance enzyme reusability, thereby reducing product isolation costs and overcoming this economic barrier. In the current study, two novel, purified lipases from Pseudomonas sp. (Pseudomonas reinekei and Pseudomonas brenneri) were entrapped in a calcium alginate matrix, with the aim of simultaneously enhancing enzyme reusability and stability. Following entrapment, the retained activity of the enzyme-alginate composite was verified by an enzymatic hydrolysis reaction of a p-nitrophenol palmitate substrate. The effect of the enzyme-alginate entrapment against various physiochemical parameters such as pH, temperature, metal ions, and solvents were subsequently examined. The entrapment was found to have minimal beneficial stability gains. However, enhanced enzyme reusability (up to 3 cycles) and stability (up to 18 days at 4°C) of the calcium alginate entrapped lipase, as indicated by residual hydrolysis of p-nitrophenol palmitate, was observed, suggesting potential roles for calcium alginate entrapped lipases in cost efficient enzyme catalysis.
HIGHLIGHTS
•Two novel lipases have been entrapped in calcium alginate for the first time.
•A statistically enhanced stability in 1M EDTA was observed following entrapment.
•The novel entrapped lipases display excellent storage stability and reusability.
- Calcium alginate
- Enzyme entrapment
- Enzyme reusability
- Enzyme stability
- Lipase
How to Cite
References
Anwar, A., Qader, S. A. U., Raiz, A., Iqbal, S. and A. Azhar, (2009). ″Calcium alginate: a support material for immobilization of proteases from newly isolated strain of Bacillus subtilis KIBGE-HAS.″ World Applied Sciences Journal, 7(10): 1281-1286.
Bagi, K., Simon, L. M. and B. Szajáni, (1997). ″Immobilization and characterization of porcine pancreas lipase.″ Enzyme and Microbial Technology, 20: 531–535.
Bhushan, I., Parshad, R., Qazi, G. N. and V. K. Gupta, (2008). ″Immobilization of Lipase by Entrapment in Ca-alginate Beads. ″ Journal of bioactiive and compatible polymers, 23(6): 552–562.
Chang, H. M. (2018). Emerging Areas in Bioengineering, Volume 1. John Wiley & Sons.
Datta, S., Christena, L. R. and Y. R. S. Rajaram, (2013). ″Enzyme immobilization: an overview on techniques and support materials. ″ 3 Biotech, 3(1): 1–9.
Glogauer, A., Martini, V. P., Faoro, H., Couto, G. H., Müller-Santos, M., Monteiro, R. A., Mitchell, D. A., de Souza, E. M., Pedrosa, F. O. and N. Krieger, (2011). ″Identification and characterization of a new true lipase isolated through metagenomic approach.″ Microbial Cell Factories, 10(1): 54-69.
Hertzberg, S., Kvittingen, L. and T. Anthonsent, (1992). ″Alginate as immobilization matrix and stabilizing agent in a two-phase liquid system: Application in lipase-catalysed reactions.″ 14: 42-47.
Homaei, A. A., Sariri, R. and R. Stevanto, (2013). ″Enzyme immobilization: an updat.″ Journal of Chemical Biology, 6: 185–205.
Kanmani, P., Ramya, S., Dhivya, R., Kaaviya Iswarya, M., Nithya Sree, V. S., Subashini, D. and K. V. Swetha, (2015). ″Rice Bran Lipase : Partial purification, immobilization in calcium alginate beads, characterization and application as a detergent additive.″ World Applied Sciences Journal, 33(6): 1052-1058.
Knezevic, Z., Bobic, S., Milutinovic, A., Obradovic, B., Mojovic, L. and B. Bugarski, (2002). ″Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system.″ Process Biochemistry, 38(3): 313–318.
Kumar, S., Yadav, R. K. and S. Negi, (2014). ″A comparative study of immobilized lipase produced from Penicillium chrysogenum SNP5 on two different anionic carriers for its pH and thermostability.″ Indian Journal of Biotechnology, 301–305.
Mohamad, N. R., Marzuki, N. H. C., Buang, N. A., Huyop, F. and R. A. Wahab, (2015). ″An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes.″ Biotechnology, Biotechnological Equipment, 29(2): 205–220.
Palmer, T. and P. L. Bonner, (2008). Enzymes: Biochemistry, biotechnology and clinical chemistry. 2nd Ed. Elsevier.
Priyanka, P., Tan, Y., Kinsella, G. K., Henehan, G. T. and B. J. Ryan, (2018). ″Solvent stable microbial lipases: Current understanding and biotechnological applications.″ Biotechnology Letters, 41(2): 203-220.
Priyanka, P., Kinsella, G., Henehan, G. T. and B. J. Ryan, (2019). ″Isolation, purification and characterization of a novel solvent stable lipase from Pseudomonas reinekei.″ Protein Expression and Purification. 153: 121–130.
Priyanka, P. (2019b). ″Biodiesel from wastewater grown microalgae using novel lipases.″ PhD thesis, Technological University Dublin, Ireland.
Sharma, M., Sharma, V. and D. K. Majumdar, (2014). ″Entrapment of α-Amylase in agar beads for biocatalysis of macromolecular substrate.″ International Scholarly Research Notices, Article ID 936129.
Shikha, S., Thakur, K. G. and M. S. Bhattacharyya, (2017). ″Facile fabrication of lipase to amine functionalized gold nanoparticles to enhance stability and activity.″ RSC Advances, 7: 42845–42855.
Talekar, S. and S. Chavare, (2012). ″Optimization of immobilization of α-amylase in alginate gel and its comparative biochemical studies with free α-amylase.″ Recent Research in Science and Technology, 4: 1–5.
Won, K., Kim, S., Kim, K. J., Park, H. W. and S. J. Moon, (2005). ″Optimization of lipase entrapment in Ca-alginate gel beads.″ Process Biochemistry, 40(6): 2149–2154.
Zhang, S., Shang, W., Yang, X., Zhang, S., Zhang, X. and J. Chen, (2013). ″Immobilization of lipase using alginate hydrogel beads and enzymatic evaluation in hydrolysis of p-nitrophenol butyrate.″ Bulletin of the Korean Chemical Society, 34(9): 2741–2746.
- Abstract Viewed: 487 times
- PDF Downloaded: 259 times