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Komitet Biotechnologii PAN ; Instytut Chemii Bioorganicznej PAN
Thermus ruber produces a-glucosidase detected in the crude extract of cell proteins. This enzyme exhibits optimum activity at 65°C and pH 6,0. The enzyme was stable within a range of pH 5.5 to 8.0 and in 65°C for 60 min. The rate of p-nitrophenol-a-D-glucopyranoside cleavage was higher than that for maltose. With maltotetraose, maltopentaose and maltohexaose, the hydrolysis rate decreased with increasing the molecular weight of the substrate. Our data suggest that the starch converting process could be improved using a-glucosidase from Thermus ruber.
2009 ; Biotechnologia, vol.85, 2 (2009)-.
0860-7796 ; oai:rcin.org.pl:72129
Biblioteka Instytutu Chemii Bioorganicznej PAN
Licencja Creative Commons Uznanie autorstwa-Na tych samych warunkach 4.0
Instytut Chemii Bioorganiczneji Polskiej Akademii Nauk
Instytut Chemii Bioorganiczneji Polskiej Akademii Nauk
Oct 2, 2020
Jun 3, 2019
548
https://rcin.org.pl./publication/94533
Sinkiewicz, Izabela Synowiecki, Józef
Sinkiewicz, Izabela Synowiecki, Józef
Borkowska, Bożenna
Ziółkowski, Piotr Babula- Skowrońska, Danuta Kaczmarek, Małgorzata Cieśla, Agata Sadowski, Jan
Grubiak, Katarzyna
Synowiecki, Józef
Nowak, Jacek K.