Purification and characterization of barley-aleurone xylanase

Autor:	E. Benjavongkulchai, Mary S. Spencer
Rok vydání:	1986
Předmět:	Gel electrophoresis Chromatography Chemistry Isoelectric focusing Sodium food and beverages chemistry.chemical_element Plant Science Isoelectric point Biochemistry Sephadex Aleurone Genetics Xylanase Hordeum vulgare
Zdroj:	Planta. 169:415-419
ISSN:	1432-2048 0032-0935
DOI:	10.1007/bf00392139
Popis:	Xylanase (β-1,4-D-xylan xylanohydrolase; EC 3.2.1.8) from aleurone layers of barley (Hordeum vulgare L. cv. Himalaya) was purified and characterized. Purification was by preparative isoelectric focusing and a Sephadex G-200 column. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the enzyme showed a single protein band with an apparent molecular weight (Mr)=34000 daltons. The isoelectric point of the enzyme was 4.6. The enzyme had maximum activity on xylan at pH 5.5 and at 35° C. It was most stable between pH 5 and 6 and at temperatures between 0 and 4° C. The Km was 0.86 mg xylan·ml(-1).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::829f4418b15d1cdb8af28c1b884d217b https://doi.org/10.1007/bf00392139 Zobrazit plný text záznamu Full text from SpringerLink