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Journal ArticleDOI

Release of periplasmic penicillin amidase from Escherichia coli by chloroform shock

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TLDR
Experimental findings show that the periplasmic penicillin amidase does not show any variation by the chloroform treatment, and this analysis was also extended to the E. coli cells grown at various concentrations of phenylacetic acid plus glucose and lactic acid.
Abstract
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.

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Citations
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Journal ArticleDOI

Whole-cell biocatalysis in organic media

TL;DR: Correlations between the cellular toxicity or the extractive capacities of different solvents and some of their physical properties have been proposed in order to minimize preliminary, solvent-selection experimental work but also to help in the understanding of the molecular mechanisms of toxicity and extraction.
Journal ArticleDOI

Penicillin acylase release from Escherichia coli cells by mechanical cell disruption and permeabilization

TL;DR: The high purity of the penicillin acylase was a consequence of the optimized differential enzyme release method which was validated by SDS gel electrophoresis.
Journal ArticleDOI

Extracellular secretion of levansucrase from Zymomonas mobilis in Escherichia coli

TL;DR: Secretion of levansucrase from Zymomonas mobilis in Escherichiacoli by glycine supplement was investigated and a significant amount of levanucrase (about 25% of total activity) was found in intact whole-cells.
Patent

Apparatus and methods for osmotically shocking cells

TL;DR: In this paper, a method for osmotically shocking cells using the first and second soluctions is also disclosed, which is a method of isolating a recombinant polypeptide of interest from a cell.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity

TL;DR: It was found that treatment of gels with dithiothreitol prior to impregnation with silver nitrate results in more reproducible staining patterns that are also qualitatively similar to those obtained with Coomassie blue.
Journal ArticleDOI

Simple, rapid, and quantitative release of periplasmic proteins by chloroform.

TL;DR: This method makes practical the analysis of the periplasmic protein complement of a large number of strains by treating cells with chloroform, and all the amino acid-binding proteins tested maintained their activity during chloro Form treatment.
Book ChapterDOI

The concept of periplasmic enzymes

TL;DR: This chapter discusses the concept of periplasmic enzymes, and it has become evident, which is nearly conclusive that a family of proteins is located at or near the surface of the cell in E. coli and certain other members of the Enterobacteriaceae.
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