Record Details

An artificial neural network analysis of porcine pancreas lipase catalysed esterification of anthranilic acid with methanol

IR@CSIR-CFTRI

View Archive Info
 
 
Field Value
 
Relation http://ir.cftri.com/1485/
PC_39_05
 
Title An artificial neural network analysis of porcine pancreas lipase catalysed esterification of anthranilic acid with methanol
 
Creator Manohar, Balaraman
Divakar, S.
 
Subject 16 Enzyme Chemistry
 
Description Artificial neural network (ANN) analysis of porcine pancreas lipase (PPL) catalysed esterification of anthranilic acid with methanol was carried out. Methanol concentration, enzyme concentration, period of incubation, buffer volume and log P-values were the five
important parameters employed. ANN analysis showed good correspondence between experimental and predicted values. The surface plots showed that methanol bound to PPL in preference to anthranilic acid. Compared to anthranilic acid (0.1 M) methanol was bound to PPL preferentially up to 0.5 M. Increase in enzyme concentration was found to enhance the extent of esterification in the concentration
range 0.5–4.5 mg/mL of PPL. A similar increase in esterification was also observed in the presence of 0.05–0.35 mL of 0.1 M phosphate buffer at pH 7.0. The positive effect of the buffer indicated that imparting ‘pH memory’ to the enzyme enhanced the extent of esterification. Esterification increased also when it was carried out in non-polar solvents like n-heptane which has a log P-value of 4.0 compared to benzene (log P: 2.0) indicating that non-polar solvents were very effective in stabilising PPL especially when they contained a small amount of 0.1 M phosphate buffer at pH 7.0.
 
Date 2005
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
Rights —
 
Identifier http://ir.cftri.com/1485/1/Process_Biochemistry_40_%282005%29_3372-3376.pdf
Manohar, Balaraman and Divakar, S. (2005) An artificial neural network analysis of porcine pancreas lipase catalysed esterification of anthranilic acid with methanol. Process Biochemistry, 40. pp. 3372-3376.