[superscript 1]H NMR Spectroscopy-Based Configurational Analysis of Mono- and Disaccharides and Detection of ß-Glucosidase Activity: An Undergraduate Biochemistry Laboratory

Autor/inn/en	Periyannan, Gopal R.; Lawrence, Barbara A.; Egan, Annie E.
Titel	[superscript 1]H NMR Spectroscopy-Based Configurational Analysis of Mono- and Disaccharides and Detection of ß-Glucosidase Activity: An Undergraduate Biochemistry Laboratory
Quelle	In: Journal of Chemical Education, 92 (2015) 7, S.1244-1249 (6 Seiten)Infoseite zur Zeitschrift PDF als Volltext Verfügbarkeit
Sprache	englisch
Dokumenttyp	gedruckt; online; Zeitschriftenaufsatz
ISSN	0021-9584
DOI	10.1021/ed500578c
Schlagwörter	Leitfaden; Unterricht; Lehrer; Spectroscopy; Science Instruction; College Science; Undergraduate Study; Biochemistry; Science Laboratories; Laboratory Experiments; Science Experiments; Molecular Structure; Teaching Methods; Scientific Concepts + Suchen Sie Ihr Suchwort? Lesson concept; Instruction; Unterrichtsentwurf; Unterrichtsprozess; Teacher; Teachers; Lehrerin; Lehrende; Spektroskopie; Teaching of science; Science education; Natural sciences Lessons; Naturwissenschaftlicher Unterricht; Grundstudium; Biochemie; Laboratory work; Laborarbeit; Teaching method; Lehrmethode; Unterrichtsmethode
Abstract	A [superscript 1]H NMR spectroscopy-based laboratory experiment explores mono- and disaccharide structural chemistry, and the enzyme-substrate specificity of glycosidic bond cleavage by ß-glucosidase towards cellobiose (ß-linked gluco-disaccharide) and maltose (a-linked gluco-disaccharide). Structural differences between cellobiose, maltose, and the glycolytic product glucose are established in terms of chemical shift changes and J-coupling constants of the anomeric proton peaks. The distinct anomeric proton signals observed in the 4.0-5.5 ppm range of glucose, cellobiose, and maltose spectra serve as a signature NMR feature to monitor the substrate specificity of ß-glucosidase towards cellobiose as a substrate. This experiment consolidates carbohydrate structural chemistry and NMR spectroscopy as applied to investigate enzyme specificity in the context of a biochemistry laboratory experiment with hands-on NMR experience for upper-division undergraduates. (As Provided).
Anmerkungen	Division of Chemical Education, Inc and ACS Publications Division of the American Chemical Society. 1155 Sixteenth Street NW, Washington, DC 20036. Tel: 800-227-5558; Tel: 202-872-4600; e-mail: eic@jce.acs.org; Web site: http://pubs.acs.org/jchemeduc
Erfasst von	ERIC (Education Resources Information Center), Washington, DC
Update	2020/1/01