Release of phenolic acids from ground rye (Secale cereale L) grain was investigated using diΓΎ erent commercial plant cell wall degrading enzyme preparations. The yields obtained were quantiΓΌed using an improved HPLC procedure developed for analysing hydroxycinnamic and hydroxybenzoic acids in ground
Glycohydrolase contamination of commercial enzymes frequently used in the preparation of fungal cell walls
β Scribed by Thomas E. Davis Jr.; Judith E. Domer
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 584 KB
- Volume
- 80
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
Commercial enzyme preparations frequently used in the preparation of fungal cell walls, viz., proteases, a lipase, and a phosphatase, were examined for the presence of contaminating glycohydrolase activity, since such activity could result not only in the removal of cytoplasmic constituents but also in the removal of portions of the wall itself. Glucosidase activities were detected in a protease of fungal origin, in a lipase from wheat germ, and in a phosphatase from potatoes. Additionally.
two commercial protease preparations from Streptomyces griseus contained p-1,3-glucanase activity in significant amounts, a third contained trace amounts of the glucanase. but a fourth was totally free of glycohydrolase activity. The protease preparations from S. griseus released laminaribiose from yeast-phase cell walls of Histoplasma capsalatum 593 CopyrIght im 1977 by Academic Press. Inc. All rIghI% ot rrproduct~~n I" any form resened.
π SIMILAR VOLUMES
An enzymatic process for upgrading the quality of canola meal (CM) by decreasing its phenolic content was investigated. The new method was based on the addition of the enzyme preparation from white-rot fungus Trametes versicolor to the meal-buffer slurry. A 98% decrease in the concentration of SAE w
A highly sensitive enzyme-linked immunosorbent assay specific to (1β3)-Ξ²-Dglucans (GBP-ELISA) has been developed using a novel (1β3)-Ξ²-D-glucan-binding protein (T-GBP), which was purified from the amebocyte lysate of the Japanese horseshoe crab, Tachypleus tridentatus. This method allowed quantitati