Lipase immobilization on hyroxypropyl methyl cellulose support and its applications for chemo-selective synthesis of β-amino ester compounds

- Lipase PFL was immobilized on HMC and used for biocatalytic application.
- Immobilized lipase was characterized by physical and biochemical techniques.
- Chemo-selective synthesis of various β-amino ester products.
- Protocol is efficiently recyclable and proposed with reaction mechanism.

The present study carried out the synthesis of β-amino ester compounds using lipase immobilized on hyroxypropyl methyl cellulose (HMC) support. Initially various lipases (biocatalysts) from different origin were immobilized and subsequently screened to obtain the robust biocatalyst. The lipase Pseudomonas fluorescence (PFL) immobilized on HMC was displayed highest lipase activity, protein content and retention of activity. The physical and biochemical characterization verified immobilization of lipase PFL on the HMC support. This immobilized biocatalyst HMC:PFL (3.5:1) was successfully applied for the practical biocatalytic applications to synthesize variety of β-amino esters. Various eight reaction parameters were optimized in details to achieve the maximum yield and chemo-selectively. The developed biocatalytic protocol was successfully applied to synthesize different industrially important β-amino esters compounds (21 substrates) with an excellent yield (>90%) and remarkable chemo selectivity (>94%). Interestingly, the immobilized HMC:PFL lipase showed 2.1-2.5 folds higher bio-catalytic activity and five times recyclability as compared to the free PFL. The plausible mechanism for lipase catalyzed synthesis of β-amino ester compounds was also proposed.

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