Abstract
Abstract A cyclodextrin glycosyltransferase (CGTase) from an alkaliphilic Bacillus sp. strain, isolated from Cuban soil, was purified with Sephadex G-50 with a yield of 66.5%. The CGTase was stable over a very wide pH range, 6.0–10, at 25°C and was most active at pH 7.5. The enzyme exhibited an optimum temperature of 60°C and was stable to 50°C for at least 8 h. The T 50 value – defined as the temperature at which 50% of the initial activity was retained–was 63°C in this enzyme. The influence of substrate or product concentration on the initial rate of CD production was studied, and the kinetic parameters were determined. The analysis of kinetic parameters K m and V max was obtained by the action of CGTase on the starch of corn with respect to β-CD, and the values were 4.1 g/L and 5.2 μM β-CD/min ml, respectively. The purified CGTase from Bacillus sp. could be used for an efficient cyclodextrin (CD) production which is the significant yield of γ- CDs.
Highlights
The increasing interest to the alkaliphilic Bacillus sp. is in connection with a great impact that these alkaliphilic microorganisms have gotten by their valuable and commercially important enzymes [1,2,3]
The purified cyclodextrin glycosyltransferase (CGTase) from Bacillus sp. could be used for an efficient cyclodextrin (CD) production which is the significant yield of γ- CDs
We report the purification and characterization of the CGTase produced by the alkaliphilic Bacillus sp
Summary
The increasing interest to the alkaliphilic Bacillus sp. is in connection with a great impact that these alkaliphilic microorganisms have gotten by their valuable and commercially important enzymes [1,2,3]. CDs are cyclic ring structure compounds consisting of six, seven, or eight glucose residues joined by α(1!4) linkages (α-, β-, and γ-CD, respectively) [9] These compounds have an exclusive ability to act as molecular containers by entrapping hydrophobic molecules in their internal cavity. Besides the ability of CGTases to catalyze the intramolecular transglycosylation reaction (cyclization), they are able to perform two intermolecular transglycosylation reactions: coupling, in which a CD ring is cleaved and transferred to a linear acceptor substrate and disproportionation, wherein two linear oligosaccharides are converted into linear oligosaccharides of different sizes These enzymes possess a weak hydrolyzing activity in which water is the glycosyl acceptor [14, 15].
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