Kinetic and docking study of synthesis of glyceryl monostearate by immobilized lipase in non-aqueous media

• Main Authors: Jawale, Priyanka V., Bhanage, Bhalchandra M.
• Format: Other Non-Article Part of Journal/Newspaper
• Language: unknown
• Published: Taylor & Francis 2021
• Subjects: Biophysics; Biochemistry; Molecular Biology; Biotechnology; 39999 Chemical Sciences not elsewhere classified; FOS Chemical sciences; Sociology; FOS Sociology; 69999 Biological Sciences not elsewhere classified; FOS Biological sciences; 110309 Infectious Diseases; FOS Health sciences; Rugosa; Antarc*; Antarctica
• Online Access: https://dx.doi.org/10.6084/m9.figshare.17135169.v1; https://tandf.figshare.com/articles/journal_contribution/Kinetic_and_docking_study_of_synthesis_of_glyceryl_monostearate_by_immobilized_lipase_in_non-aqueous_media/17135169/1

Glyceryl monostearate is extensively used as an emulsifier in many industries. Mono acylation of glycerol was carried out by utilizing immobilized Candida antarctica lipase B (Cal B) as a biocatalyst and vinyl stearate as an acyl donor. Different reaction parameters, such as selection of lipases from various sources (like Candida antarctica , Candida rugosa, and Mucor meihei ) and their quantity, shaking speed, temperature, substrate concentration, and reusability were studied in detail to achieve excellent conversion. Overall, 98% conversion of glycerol was obtained at a mole ratio of 1:1 of glycerol to vinyl stearate, using 12 mg of immobilized Cal B at 45 °C for 3 h. The mechanism of the given reaction was anticipated based on the results of the Lineweaver-Burk plots. It was found that the reaction followed the Ping-Pong Bi Bi mechanism with inhibition of glycerol. As it was a kinetically controlled synthesis, different kinetic constants were estimated by non-linear regression analysis. The activation energy for Cal B was found to be 10.3 kcal/mol. Further, biocatalyst can be reused up to four catalytic cycles with an average four percent loss of activity. A molecular docking study was done to find out the confirmation of substrates and their binding positions in an enzyme. It was noticed that the reaction proceeds through acyl-enzyme complex formation followed by the transfer of that acyl group to another substrate.