Effect of counterions on the activity of lipase in cationic water-in-oil microemulsions

Debnath, Sisir ; Dasgupta, Antara ; Mitra, Rajendra Narayan ; Das, Prasanta Kumar (2006) Effect of counterions on the activity of lipase in cationic water-in-oil microemulsions Langmuir, 22 (21). pp. 8732-8740. ISSN 0743-7463

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Official URL: http://pubs.acs.org/doi/abs/10.1021/la061487d

Related URL: http://dx.doi.org/10.1021/la061487d


This paper delineates how the different counterions affect the physicochemical properties of the aqueous aggregates and thereby the lipase activities at the interface of cationic water-in-oil microemulsions. To this end, we have synthesized a series of cetyltrimethylammonium-based surfactants, 1−14, having aliphatic, aliphatic with aromatic substitution at the α position, and aromatic carboxylate anion as the counterion. The physicochemical characterizations of these aqueous aggregates were done by conductometric, tensiometric, fluorometric techniques to determine counterion binding (β), critical micelle concentration (cmc), and micropolarity at the microenvironment. It has been found that the activity of lipase mainly increases with hydrophobicity (which is directly proportional to the counterion binding (β) of the surfactant) of the counterion and reaches a maximum when the β value is around 0.5. Increase in hydrophobicity as well as β leads to the attachment of more counterions at interface resulting in enhancement of interfacial area. Consequently, the enzyme may attain flexible secondary conformation at the augmented surface area and also allow larger population of substrates and enzyme molecules at the interface leading to the enhancement in lipase activity. After an optimum value of β, further increase probably produces a steric crowding at the interface, hindering the smooth occupancy of enzyme and the substrate in this region leading to decrease of enzyme activity, while molecular surface area of the counterion did not show any virtual influence on the lipase activity. Thus, the variation in the counterion structure and hydrophobicity plays a crucial role in modulating the lipase activity.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:108742
Deposited On:01 Feb 2018 11:19
Last Modified:01 Feb 2018 11:19

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