Purification and properties of a hyperthermoactive α-amylase from the archaeobacterium Pyrococcus woesei

The cultivation of the hyperthermophilic archaeobacterium Pyrococcus woesei on starch under continuous gassing (80% H sub(2):20% CO sub(2)) caused the formation of 250 U/l of an extremely thermoactive and thermostable alpha -amylase. In a complex medium without elemental sulphur under 80% N sub(2) a...

Full description

Saved in:
Bibliographic Details
Published in:Archives of microbiology 1991-06, Vol.155 (6), p.572-578
Main Authors: KOCH, R, SPREINAT, A, LEMKE, K, ANTRANIKIAN, G
Format: Article
Language:English
Subjects:
alpha -amylase
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
thermophilic bacteria
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The cultivation of the hyperthermophilic archaeobacterium Pyrococcus woesei on starch under continuous gassing (80% H sub(2):20% CO sub(2)) caused the formation of 250 U/l of an extremely thermoactive and thermostable alpha -amylase. In a complex medium without elemental sulphur under 80% N sub(2) and 20% CO sub(2) atmosphere enzyme production could be elevated up to 1000 U/l. Pyrococcus woesei) grew preferentially on poly- and oligosaccharides. The amylolytic enzyme formation was constitutive. Enzyme production was also observed in continuous culture at dilution rates from 0.1 to 0.4 h super(-1). A 20-fold enrichment of alpha -amylase was achieved after adsorption of the enzyme onto starch and its desorption by preparative gel electrophoresis. The alpha -amylase consisted of a single subunit with a molecular mass of 70,000 and was catalytically active at a temperature range between 40 degree C and 130 degree C.
ISSN:0302-8933
1432-072X
DOI:10.1007/BF00245352