ISSN:
1573-6776
Keywords:
α-amylase
;
starch biodegradation
;
Thermomyces lanuginosus
;
thermophilic fungi
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract α-Amylases from the thermophilic fungus, Thermomyces lanuginosus ATCC 34626 (wild and mutant strains), were purified to homogeneity by a simple procedure including, consecutively, precipitation with ice-cold 2-propanol, anion-exchange and molecular-sieve chromatographic methods. The molecular masses of the purified α-amylases (both with pI values of 3.0) were 58 kDa by SDS-PAGE. The optimal pH of α-amylase activity was 5.0 for the wild enzyme and 4.5 for the mutant one. 1-Cyclohexyl-3-(2-morpholinyl-4-ethyl)-carbodiimide (40–100 mM) and N-bromosuccinimide (0.1–1 mM) inhibited the enzymes, suggesting the involvement of carboxylic groups and tryptophan residues in the catalytic process.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1005685226480