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Rhamnogalacturonan alpha-L-rhamnopyranohydrolase. A novel enzyme specific for the terminal nonreducing rhamnosyl unit in rhamnogalacturonan regions of pectin.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Mutter, Margien Beldman, Gerrit Schols, H. A. Voragen, Alphons G. J. |
| Copyright Year | 1994 |
| Abstract | 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 the alpha-1,2- or alpha-1,6-linkage to beta-D-glucose. The pnp-rhamnohydrolase had a molecular mass of 87 kD (sodium dodecyl sulfate-polyacrylamide gel electrophoresis), a pH optimum of 5.5 to 6, a temperature optimum of 60 degrees C, and a specific activity toward pnp-alpha-L-rhamnopyranoside (pnp-Rha) of 13 units mg-1 protein. The second rhamnohydrolase, on the contrary, was active toward rhamnogalacturonan (RG) fragments, releasing Rha, and was therefore termed RG-rhamnohydrolase. The RG-rhamnohydrolase had a molecular mass of 84 kD, a pH optimum of 4, a temperature optimum of 60 degrees C, and a specific activity toward RG oligomers of 60 units mg-1 protein. The RG-rhamnohydrolase liberated Rha from the nonreducing end of the RG chain and appeared specific for the alpha-1,4-linkage to alpha-D-galacturonic acid. The enzyme was hindered when this terminal Rha residue was substituted at the 4-position by a beta-D-galactose. The results so far obtained did not indicate particular preference of the enzyme for low or high molecular mass RG fragments. From the results it can be concluded that a new enzyme, an RG alpha-L-rhamnopyranohydrolase, has been isolated with high specificity toward RG regions of pectin. |
| Starting Page | 1067 |
| Ending Page | 1067 |
| Page Count | 1 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.plantphysiol.org/content/plantphysiol/106/1/241.full.pdf |
| PubMed reference number | 7972516v1 |
| Volume Number | 106 |
| Issue Number | 1 |
| Journal | Plant physiology |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | DHX9 gene Galactose Gel Electrophoresis (lab technique) Glucose Metabolism Disorders HCL2 gene Hesperidin Mg-5'-Adenylylimidodiphosphate Molecular Mass Polyacrylamide Gel Electrophoresis RG 83852 monoclonal antibody SDS-PAGE Sodium Dodecyl Sulfate Substrate Specificity Thioctic Acid beta Thalassemia naringin pectin polyacrylamide gels type I interferon receptor |
| Content Type | Text |
| Resource Type | Article |
