For improved biosynthesis of penicillin amidase by E. coli, NCIM 2400, the participation of different carboxylic acids and polyols has been studied in association with the effect of phenylacetic acid. A modified defined medium has been devised for this purpose. © 1991 Springer-Verlag.

T Panda

Department Of Chemical Engineering

P. S.R. Babu

carboxylic acid

penicillin amidase

Phenylacetic acid

polyol

article

Escherichia coli

nonhuman

IIT Madras is a public technical and research university located in Chennai, Tamil Nadu. Founded in 1959, it is recognised as an Institute of National Importance.

IIT Madras has been ranked as the top engineering institute in India for four years in a row by the National Institutional Ranking Framework of the MHRD

It currently offers undergraduate, postgraduate and research degrees across 16 disciplines in Engineering, Sciences, Humanities and Management. About 596 faculty belonging to science and engineering departments and centres of the Institute are engaged in teaching, research and industrial consultancy.

IIT Madras

The role of phenylacetic acid in biosynthesis of penicillin amidase in E. coli

Bioprocess Engineering

Penicillin amidase is a periplasmic enzyme in Escherichia coli. Conventionally, the periplasmic enzymes are released into the medium by osmotic shock which is tedious involving a number of centrifugation steps. The present communication deals with a simple technique for the release of penicillin amidase by chloroform shock. Experimental findings show that the periplasmic penicillin amidase does not show any variation by the chloroform treatment. This analysis was also extended to the E. coli cells grown at various concentrations of phenylacetic acid, optimal concentration of phenylacetic acid plus glucose and lactic acid.

Release of periplasmic penicillin amidase from Escherichia coli by chloroform shock

A method for catalyst development has been suggested for immobilizing whole E. coli cells containing penicillin amidase. Conventional methods have limitations, such as permeation of substrate and product through cellular membranes, leaching of protein and other cellular components into the reaction phase, lower specific activity compared to immobilized enzyme system, etc. The whole cell immobilization technique has been optimized for different process parameters. The most suitable conditions for this process were pH, 4.25; cell concentration, 3.75%; concentration of glutaraldehyde, 1.5%; level of bovine serum albumin as additional support, 2 mg ml-1. The reaction was continued for 2 h. The granular catalyst has good mechanical strength, low protein leachability, and high retention of penicillin amidase activity. © 1991.

Enzyme and Microbial Technology

Studies on improved techniques for immobilizing and stabilizing penicillin amidase associated with E. coli cells

Journal of Applied Chemistry

Production of Escherichia coli as a source of nucleic acids

Asian Theatre Journal

The Bhāsa Festival, Trivandrum, India

Enzyme Engineering

Immobilization of Whole Microbial Cells for the Production of 6- Amino Penicillanic Acid

Biochimica et Biophysica Acta (BBA) - Enzymology

The isolation and kinetics of penicillin amidase from Escherichia coli

Journal	Data powered by TypesetBioprocess Engineering
Publisher	Data powered by TypesetSpringer-Verlag
ISSN	0178515X
Open Access	No