Article

Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: Enzyme characteristics and stability

Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla 171005, HP, India.
Bioresource Technology (Impact Factor: 5.04). 06/2008; 99(7):2566-70. DOI: 10.1016/j.biortech.2007.04.042
Source: PubMed

ABSTRACT An extracellular alkaline lipase of a thermo tolerant Bacillus coagulans BTS-3 was immobilized onto glutaraldehyde activated Nylon-6 by covalent binding. Under optimum conditions, the immobilization yielded a protein loading of 228 microg/g of Nylon-6. Immobilized enzyme showed maximum activity at a temperature of 55 degrees C and pH 7.5. The enzyme was stable between pH 7.5-9.5. It retained 88% of its original activity at 55 degrees C for 2h and also retained 85% of its original activity after eight cycles of hydrolysis of p-NPP. Kinetic parameters Km and Vmax were found to be 4mM and 10 micromol/min/ml, respectively. The influence of organic solvents on the catalytic activity of immobilized enzyme was also evaluated. The bound lipase showed enhanced activity when exposed to n-heptane. The substrate specificity of immobilized enzyme revealed more efficient hydrolysis of higher carbon length (C-16) ester than other ones.

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    • "Nevertheless, this problem can be overcome by enzyme immobilization , which enhances thermal and operational stabilities , ease of handling, and prevention of aggregation and autolysis. Besides, immobilized lipases (IE) on solid support allow recoverability and reuse thus significantly reducing operational costs of industrial processes [4] [5] [6] [7] [8]. An immobilization process involving hydrophobic binding of lipases by adsorption has proved success due to the enzyme affinity for water/oil interfaces [6] [9] [10]. "
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