Abstract
A cyclodextrin glucanotransferase (EC 2.4.1.19) (CGTase) from Bacillus autolyticus was purified to homogeneous, and its properties were investigated. The molecular weight was estimated to be 68,000 by gel chromatography and 70,000 by SDS-PAGE. The optimum pH of the enzyme was 5.0–6.0. The optimum reaction temperature was 60°C. HgCl 2 inhibited the enzyme activity completely. The enzyme formed mainly β-cyclodextrin (β-CD) with a small amount of α-cyclodextrin (α-CD) and γ-cyclodextrin (γ-CD) from potato starch. Ethanol and Triton X-100 enhanced the specificity and yield of β-CD production. Especially, the effect of Triton X-100 was remarkable. With 4% (v/v) Triton X-100, β-CD was formed in a maximum yield of 56% from 10% (w/v) potato starch with negligible amounts of α-CD and γ-CD (both yields were less than 1%) at a later stage of the reaction.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
