Formation of Disulfide-Bridged Dimers During Thermoinactivation of Glucoamylase from Aspergillus Niger
Autor: | Bence Asbóth, Zsuzsanna Sasvári |
---|---|
Rok vydání: | 1998 |
Předmět: |
chemistry.chemical_classification
biology Starch Stereochemistry Dimer Aspergillus niger Bioengineering biology.organism_classification Cleavage (embryo) Applied Microbiology and Biotechnology Biochemistry chemistry.chemical_compound Enzyme chemistry Intramolecular force Cyanogen bromide Biotechnology Thermostability |
Zdroj: | Enzyme and Microbial Technology. 22:466-470 |
ISSN: | 0141-0229 |
DOI: | 10.1016/s0141-0229(97)00235-4 |
Popis: | In the course of thermoinactivation of the smaller izoenzyme and of a truncated form of glucoamylase from Aspergillus niger, we observed the formation of disulfide-linked dimers. Molecular modelling studies indicated and the cyanogen bromide cleavage pattern gave corroborating evidence that it is the Cys 222–449 intramolecular disulfide bond that opens up and reforms intermolecularly to yield dimers. Since the dimer displayed the same activity as the native enzyme toward maltopentaose and soluble starch and showed increased thermostability at temperatures above 68°C, it appears a prospective candidate for industrial usage. |
Databáze: | OpenAIRE |
Externí odkaz: |