Abstract
Limit dextrinase is one of three main amylases in malted barley, which plays a significant role during the mashing stage of brewing. Due to very low content and similar properties compared to other amylases in malted barley, limit dextrinase is hard to separate effectively. Our work had been directed towards the extraction and purification of limit dextrinase from malted barley. Final products were obtained through fraction precipitation with ammonium sulfate and column chromatography, and purified limit dextrinase acquired a high purity of 31.23 times as much as that of crude extracts. The previous results were also confirmed by sodiumdodecyl sulphate poly-acrylamide gel electrophoresis (SDS-PAGE) revealing a single band of protein (~97KDa). Effect of temperature, pH value, and metal ion on hydrolysis characterization of limit dextrinase was investigated. The results indicated that the maximum activity of purified samples changed significantly compared with that of crude extracts. The activity of purified limit dextrinase could be activated by lower concentration of Mg2+、Ca2+、Mn2+ and inhibited by the action of Zn2+、Fe2+. But this influence was not so obvious for K+.
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.
