Enhancement of operation and storage stability of glucoamylase fromAspergillus awamoriby a protease inhibitor preparation

Autor:	L. Gubicza, Tamás Fráter, Katalin Bélafi-Bakó, Nándor Nemestóthy
Rok vydání:	2005
Předmět:	chemistry.chemical_classification Proteases Chromatography Starch Substrate (chemistry) Biochemistry Catalysis Protease inhibitor (biology) chemistry.chemical_compound Hydrolysis Enzyme chemistry medicine Fermentation Aspergillus awamori Biotechnology medicine.drug
Zdroj:	Biocatalysis and Biotransformation. 23:281-284
ISSN:	1029-2446 1024-2422
DOI:	10.1080/03081070500192850
Popis:	Glucoamylase was produced extracellularly by fermentation of strain Aspergillus awamori, which had been genetically modified to have high-level glucoamylase activity. Initial experiments showed that the enzyme deactivated quickly, with a half-life of less than 6 days even stored at 5°C. A possible reason for the rapid deactivation was the presence of proteases, attacking and degrading the glucoamylase. Therefore a liquid protease inhibitor cocktail (Sigma, USA) was selected and applied to enhance the stability of the enzyme. The activity of the enzyme (stored at 5°C) measured by the Schoorl-method with starch as substrate showed that the cocktail was effective with the enzyme maintaining 95% of its initial storage activity for almost one year. The enzyme preparation has been used for starch hydrolysis in a flat-sheet membrane bioreactor at 60°C to manufacture glucose solution and its operation stability extended by using the cocktail.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::4e5d2f5ae7a8736656646b1da2a6ba3d https://doi.org/10.1080/03081070500192850 Zobrazit plný text záznamu