Purification and characterization of three (14)-beta-d-xylan endohydrolases from germinated barley
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چکیده
منابع مشابه
Purification and characterization of two 1,4-beta-xylan endohydrolases from the rumen fungus Neocallimastix frontalis.
Two beta-endoxylanases produced by Neocallimastix frontalis have been purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. Xylanase I is a nonglycosylated protein with an apparent molecular mass of 45 kDa. Xylanase II is a glycoprotein with an apparent molecular mass of 70 kDa. The pH optima of these enzymes were 5.5 and 6, respectively, and the temperatu...
متن کاملBarley beta-D-glucan exohydrolases with beta-D-glucosidase activity. Purification, characterization, and determination of primary structure from a cDNA clone.
Two beta-glucan exohydrolases of apparent molecular masses 69,000 and 71,000 Da have been purified from extracts of 8-day germinated barley grains and are designated isoenzymes ExoI and ExoII, respectively. The sequences of their first 52 NH2-terminal amino acids show 64% positional identity. Both enzymes hydrolyze the (1,3)-beta-glucan, laminarin, but also hydrolyze (1,3;1,4)-beta-glucan and 4...
متن کاملPurification and Characterization of Three Soluble Invertases from Barley ( Hordeum vulgare 1 . ) Leaves '
Three soluble isoforms of invertase (8-fructofuranosidase; EC 3.2.1.26) were purified from 7-d-old primary leaves of barley (Hordeum vurgare 1.). lnvertase I, a monomeric protein of 64 kD, was purified to apparent homogeneity as shown by sodium dodecylsulfate-polyacrylamide gel electrophoresis. lnvertases IIA and IIB, multimeric proteins with molecular masses of 116 and 155 kD, were purified 78...
متن کاملPartial purification and characterization of endoproteinases from senescing barley leaves.
Two major endoproteinases were purified from senescing primary barley leaves. The major enzyme (EP(1)) appeared to be a thiol proteinase and accounted for about 85% of the total proteolytic activity measured in vitro. This proteinase was purified 5,800-fold and had a molecular weight of 28,300. It was highly unstable in the absence of dithiothreitol or at a pH greater than 7.5. Leupeptin, at a ...
متن کاملISOLATION AND PROPERTIES OF CRYSTALLINE (r-AMYLASE FROM GERMINATED BARLEY*
The isolation of crystalline ar-amylase has been reported in a preliminary communication (1). Details of the method of isolation, behavior of the fractions leading to crystallization, and some properties of the crystalline material are reported here. This material constitutes the first instance of the crystallization of an cu-amylase from a higher plant and is probably the only protein crystall...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1989
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1989.tb15146.x