High performance liquid chromatography analysis and quantitation of chitinolytic products of CDC group EF-4a

dc.contributor.advisorWarnes, Carl E.en_US
dc.contributor.authorBaker-Ellis, Judyen_US
dc.date.accessioned2011-06-03T19:34:03Z
dc.date.available2011-06-03T19:34:03Z
dc.date.created1985en_US
dc.date.issued1985
dc.description.abstractA chitinolytic organism was cultured from a lotic habitat in central Indiana. It was isolated on the basis of its hydrolytic activity on chitin agar. It was subsequently identified as EF-4a. The chitinases of the EF-4a were isolated, purified and concentrated. A colloidal chitin suspension was then incubated with the enzyme. Samplings were taken at one minute, one hour and 24 hours. The samplings were filtered through a Swinney filtration unit and immediately after applied to a Beckman Ultrasil Amino column. It was eluted with acetonitrile: water (75:25) at a flow rate of 2 ml/min. The absorbance at 214 nm was monitored using the Beckman 160 UV detector. The chromatographs were analyzed for product elaboration. It was observed that EF-4a produced soluble, extracellular enzymes. The enzymes were a chitinase-chitobiase complex. The enzymes' action on chitin was immediate. There were varying reaction products including G1cN, GlcNAc, chitobiose, chitotriose and higher order oligomers. There was also chromatographic evidence suggesting a and B anomers of these saccharides.
dc.description.degreeThesis (M.S.)
dc.format.extentv, 54 leaves : ill. ; 28 cm.en_US
dc.identifierLD2489.Z78 1985 .B34en_US
dc.identifier.cardcat-urlhttp://liblink.bsu.edu/catkey/443555en_US
dc.identifier.urihttp://cardinalscholar.bsu.edu/handle/20.500.14291/183132
dc.sourceVirtual Pressen_US
dc.subject.lcshChitin.en_US
dc.subject.lcshChromatographic analysis.en_US
dc.titleHigh performance liquid chromatography analysis and quantitation of chitinolytic products of CDC group EF-4aen_US
Files
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.98 KB
Format:
Item-specific license agreed upon to submission
Description:
Collections