Rhamnogalacturonan lyase: a pectin modification enzyme of higher plants
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منابع مشابه
Rhamnogalacturonan alpha-L-rhamnopyranohydrolase. A novel enzyme specific for the terminal nonreducing rhamnosyl unit in rhamnogalacturonan regions of pectin.
Two alpha-L-rhamnohydrolases with different substrate specificities were isolated from a commercial preparation produced by Aspergillus aculeatus. The first rhamnohydrolase was active toward p-nitrophenyl-alpha-L- rhamnopyranoside, naringin, and hesperidin and was termed p-nitrophenyl-alpha-L-rhamnopyranohydrolase (pnp-rhamnohydrolase). From the data collected, the enzyme seemed specific for th...
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A simple method was developed for fast identification of pectin, based on a recombinant endopectate lyase cloned from Aspergillus niger. When pectin was demethylated and treated with pectate lyase, beta-elimination occurred, resulting in a double bond between C-4 and C-5 in the galacturonic acid residue of the released nonreducing end. The formation of double bonds produced an increase in light...
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Clostridium cellulolyticum secretes large multienzymatic complexes with plant cell wall-degrading activities named cellulosomes. Most of the genes encoding cellulosomal components are located in a large gene cluster: cipC-cel48F-cel8C-cel9G-cel9E-orfX-cel9H-cel9J-man5K-cel9M. Downstream of the cel9M gene, a new open reading frame was discovered and named rgl11Y. Amino acid sequence analysis ind...
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In 1957 Glaser (1) obtained a particulate fraction from Acetobatter xylinum which catalyzed the incorporation of the glucosyl moiety of uridine diphosphate n-glucose into cellulose. It seemed probable that this most important structural polysaccharide of higher plants was synthesized by a similar mechanism, but attempts to bring about its formation from uridine diphosphate u-glucose by enzyme s...
متن کاملPectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin.
The gene yvpA from Bacillus subtilis was cloned and expressed in Escherichia coli. It encoded a pectate lyase of 221 amino acids that was denominated PelC. The heterologously expressed enzyme was purified by His-tag affinity chromatography and characterized. PelC depolymerized polygalacturonate and pectins of methyl esterification degree from 22 % to 89 %, exhibiting maximum activity on 22 % es...
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ژورنال
عنوان ژورنال: Emirates Journal of Food and Agriculture
سال: 2018
ISSN: 2079-0538,2079-052X
DOI: 10.9755/ejfa.2018.v30.i11.1858