title: Complexation of alkyl glycosides with α-cyclodextrin can have drastically different effects on their conversion by glycoside hydrolases.
abstract: Substrates present in aggregated forms, such as micelles, are often poorly converted by enzymes. Alkyl glycosides constitute typical examples and the critical micelle concentration (CMC) decreases with increasing length of the alkyl group. In this study, possibilities to hydrolyse alkyl glycosides by glycoside hydrolases were explored, and α-cyclodextrin was used as an agent to form inclusion complexes with the alkyl glycosides, thereby preventing micelle formation. The cyclodextrin complexes were accepted as substrates by the enzymes to variable extent. The β-glucosidases originating from Thermotoga neapolitana (Tn Bgl3B) and from almond were not at all able to hydrolyse alkyl β-glucosides in the presence of 100mM α-cyclodextrin. However, Aspergillus niger amyloglucosidase readily accepted the complexes as substrates. In reactions involving decyl and dodecyl maltosides, the presence of 100mM α-cyclodextrin caused an increase in reaction rate in most cases, especially at high substrate concentrations. Surprisingly, the amyloglucosidase-catalyzed hydrolysis of octyl-β-maltoside to glucose and β-octylglucoside was faster in the presence of α-cyclodextrin than without, even at substrate concentrations below CMC. A possible explanation of the observed rate enhancement is that binding sites on the carbohydrate binding domain of amyloglucosidase, known to bind cyclodextrins, help to guide the alkyl glycoside-cyclodextrin complex to the active site, and thereby promote its conversion.
authors.affiliation: Department of Biotechnology, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.
authors.forename: Mohd Younis
authors.initials: MY
authors.lastname: Rather
authors.affiliation: Department of Biotechnology, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.
authors.forename: Eva
authors.initials: E
authors.lastname: Nordberg Karlsson
authors.affiliation: Department of Biotechnology, Lund University, P.O. Box 124, SE-22100 Lund, Sweden. Electronic address: Patrick.Adlercreutz@biotek.lu.se.
authors.forename: Patrick
authors.initials: P
authors.lastname: Adlercreutz
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000737:chemistry*; D006027:Glycosides / Q000737:chemistry*; D006868:Hydrolysis; D008823:Micelles; D010940:Plant Proteins / Q000737:chemistry; D000068181:Prunus dulcis / Q000201:enzymology; D046949:Thermotoga neapolitana / Q000201:enzymology; D047391:alpha-Cyclodextrins / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D006027:Glycosides; D008823:Micelles; D010940:Plant Proteins; D047391:alpha-Cyclodextrins; D006026:Glycoside Hydrolases; C032613:alpha-cyclodextrin
keywords: Alkyl glycoside; Amyloglucosidase; Complexation; Micelle; α-Cyclodextrin, β-Glucosidase