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PubMed1997

Evaluation of the activities of eight lysosomal hydrolases in sera of humans, rats and pigs of different ages.

The activities of 21 enzymes (belonging to four classes of enzymes) involved in different metabolic pathways were assayed in blood sera of healthy young and adult/elderly groups of humans, rats and pigs, to determine whether activity changes coinciding with changes in age and aging could be detected. In all three species analysed, measurable activities (performed by highly specific and sensitive techniques, generally spectrofluorimetric procedures) were found, usually following a decreasing order of: among glycosidases, beta-N-acetylglucosaminidase (NAG) > alpha-L-fucosidase > alpha-mannosidase > beta-glucuronidase > beta-galactosidase > alpha-galactosidase. In addition, among esterases very high values were found for arylesterase and acid phosphatase. By contrast, no measurable activity was found for the remaining enzymes assayed (8 hydrolases, 1 oxidoreductase, 3 transferases and 1 lyase). In the elderly group of humans, significantly higher activities (P < or = 0.05) were found for NAG, alpha-mannosidase and beta-glucuronidase in comparison to the adult and young groups. However, several activities in rats and all activities in pigs decreased with age. In conclusion, differences in the activities of 6 lysosomal glycosidases and 2 esterases (but no significant differences for another 13 enzymes belonging to several enzyme classes) are found in the sera of healthy humans, rats and pigs. These differences coincide with changes observed in aging.

Acid Phosphatase↗
PubMed1976

Pectic enzymes.

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Bacteria↗
PubMed2002

Enzymatic solubilization of arabinoxylans from isolated rye pentosans and rye flour by different endo-xylanases and other hydrolyzing enzymes. Effect of a fungal caccase on the flour extracts oxidative gelation.

Water-extractable (WEP) and water-unextractable (WUP) pentosans were isolated from a rye flour. The effect of a commercial enzyme preparation, Grindamyl S 100 (GS100), containing pentosanase activities, was investigated on WEP, WUP, a mix of WEP and WUP, and the rye flour, with the aim to monitor the solubilization and depolymerization of high molecular weight arabinoxylans and the effect on the viscosity of the reaction medium. The effects of other hydrolyzing enzymes were also tested. Three xylanases were used: xylanase 1 (Xyl-1) from Aspergillus niger, the main activity present in GS100; xylanase 2 (Xyl-2) from Talaromyces emersonii; and xylanase 3 (Xyl-3) from Bacillus subtilis. Xyl-3 was used in combination with Xyl-1, (1,4)-beta-D-arabinoxylan arabinofuranohydrolase, endo-beta-D-glucanase, or ferulate esterase from A. niger, but no synergism was observed. GS100 and xylanases increased the arabinoxylan solubilization, Xyl-3 and Xyl-1 being those that presented the best yields of extraction without extensive depolymerization of water-extractable arabinoxylans. Both xylanases were affected by an inhibitor in rye flour. Flour treated with hot ethanol was used to study the oxidative gelation of flour extracts treated with xylanases, in the presence of laccase from Pycnoporus cinnabarinus. Two doses of xylanases were tested (0.5 and 2.5 units). Only the flour extracts treated with 0.5 unit of Xyl-1 thickened.

Carboxylic Ester Hydrolases↗