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Journal ArticleDOI

Catabolite repression of hydrolases in Aspergillus niger

TLDR
It is suggested that catabolite repression of polygalacturonase occurs at the level of translation and that of acid protease at transcription in an adenine-requiring mutant of Aspergillus niger.
Abstract
A comparative study was made on catabolite repression of acid protease and polygalacturonase in an adenine-requiring mutant of Aspergillus niger. Both enzymes are inducible and accumulated extracellularly after cessation of growth caused by adenine starvation. Addition of glucose, fructose, or intermediates of glycolysis, but not tricarboxylic acid cycle intermediates, depressed the formation of both enzymes. Catabolite repression of polygalacturonase by glucose occurred quickly and was almost complete. However, acid protease was only partly repressed even after several hours. Formation of polygalacturonase in the presence of actinomycin S3 or during deinduction was repressed by glucose, whereas that of acid protease was not. In the course of induction of acid protease by peptone, glucose did not affect the length of the induction lag period and the rate of acid protease formation decreased by glucose was not restored by the addition of large amounts of inducer. From these results, we suggest that catabolite repression of polygalacturonase occurs at the level of translation and that of acid protease at transcription.

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Citations
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Journal ArticleDOI

Stimulation of the production of extracellular pectinolytic activities of Aspergillus sp. by galacturonic acid and glucose addition

TL;DR: The results showed that a differential response in the production of the activities was produced, suggesting that galacturonic acid participates in the induction of pectinolytic activities of Aspergillus sp.
Book ChapterDOI

Increasing yields of extracellular enzymes.

TL;DR: This chapter discusses the current rationales and methodologies employed to increase the extracellular enzyme yields through strain selection, environmental control, genetic regulatory controls, genetic recombination, and gene amplification techniques.
Journal ArticleDOI

Carbon Source Control of Cellobiohydrolase I and II Formation by Trichoderma reesei.

TL;DR: Northern (RNA) hybridization with full copies of cbh1 and cbh2 genes indicated that the control of CBH I and CBH II biosyntheses by the carbon source operates mainly at the pretranslational level.
Journal ArticleDOI

Application of fed-batch cultures in the production of extracellular pectinases by Aspergillus sp.

TL;DR: The production of extracellular pectinases by Aspergillus sp.
Journal ArticleDOI

Catabolite repression of the synthesis of inducible polygalacturonase and pectinesterase byAspergillus niger sp.

TL;DR: The synthesis of pectinesterase and polygalacturonase by a strain of Aspergillus niger isolated from rotten lemons was repressed by glucose, even in the presence of the inducer, suggesting that repression occurs at the translational level.
References
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Journal ArticleDOI

Disc electrophoresis – ii method and application to human serum proteins*

TL;DR: The technique of disc electrophoresis has been presented, including a discussion of the technical variables with special reference to the separation of protein fractions of normal human serum.
Journal Article

Methods in Enzymology.

TL;DR: This volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of the instrument and its ancillary tools are simply and well presented.
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The lactose operon

Journal ArticleDOI

Stimulation of tryptophanase synthesis in Escherichia coli by cyclic 3',5'-adenosine monophosphate.

TL;DR: Cyclic 3',5'-AMP was shown to increase the rate of tryptophanase synthesis in Escherichia coli treated with tris(hydroxymethyl)aminomethane and ethylenediaminetetraacetic acid and induced with tryphan as mentioned in this paper.
Book ChapterDOI

[5] Polymers coupled to agarose as stable and high capacity spacers

Meir Wilchek, +1 more
TL;DR: For successful use of affinity chromatography, the polymer-bound ligand must be sufficiently distant from the polymer surface to minimize steric interference by introducing a spacer between the solid matrix and the ligand.
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