The stabilization of enzymes against inactivation is a major challenge that limits their application in industry and materials. Conjugation of enzymes to the polymer poly(acrylic acid) (PAA) or to other enzymes such as bovine serum albumin via 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) is an excellent way of ‘armoring’ the enzyme. Laccase, a copper-containing oxidase enzyme often used in biofuel cells, textile dye removal, food industry, and wastewater treatment has been interlocked in cellulose via this approach. Once conjugated in cellulose fibers of the paper, the enzyme is protected against denaturing and does not wash off when immersed in a solution. The significance of this conjugation method is that it doesn’t require any complex methods or toxic materials, the entire biocatalyst is made of biodegradable materials, the method is not enzyme-specific, the enzyme is stable long-term, and the amount of enzyme loaded per gram of cellulose is much higher compared to other methods, making it an attractive and scalable method for industrial applications. Interlocked enzyme retained activities to a significant extent.

Stable-on-the-table enzymes: Interlocking of laccase in Whatman filter paper

253rd National Meeting (2017)

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