This research work aimed to increase the stability and activity of an industrially important enzyme, Candida antarctica lipase B (CalB). In our research work, we modified CalB with hydrophilic and hydrophobic polymers such as acrylamide (Am); dimethyl acrylamide (DMAm); block polymers of acrylamide and N-isopropyl acrylamide (NIPAm); a block polymer of acrylamide and a mixture of N-isopropyl acrylamide (NIPAM) and N-isobutoxy methyl acrylamide (NIBMA); 2-acrylamido-2-methylpropane sulfonic acid (AMPSA); a mixed polymer of DMAm and AMPSA and N, N-dimethylaminopropyl-acrylamide (DMAPA). To observe the effect of different lengths of polymers on CalB, we synthesized our polymers in three different chain lengths: DP10, DP25 and DP50 using reversible addition-fragmentation chain transfer (RAFT) polymerization method. We found a significant enhancement of activity for acrylamide (Am) and dimethyl acrylamide (DMAm) conjugates, indicating a probable noncovalent interaction of the polymers with the substrate. This activity enhancement was also found to be relatively preserved in 25% and 75% ethanol solvent systems. On the contrary, hydrophobic as well as anionic polymers were not able to preserve the activity in these solvent systems. In our study, we also observed a greater stability of the conjugates in different organic solvent systems including 75% acetonitrile, 75% ethanol, 50% ethanol and 25% ethanol solvent systems. Thus, this study gives us an insight into the advances of lipase production which can improve the activity and stability of lipase in presence of denaturing organic solvents.

Polymer modification of lipases, substrate interactions, and potential inhibition

ACS Fall 2021

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