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1.
Lett Appl Microbiol ; 65(1): 82-89, 2017 Jul.
Article in English | MEDLINE | ID: mdl-28426165

ABSTRACT

Honey originating from different floral sources exhibits the broad spectrum of antibacterial activity as a result of the presence of hydrogen peroxide as well as nonperoxide bioactive compounds. The mechanisms of antibacterial activity of Polish melilot honey were investigated for the first time. Polish melilot honey samples (Melilotus albus biennial = 3 and annual = 5, Melilotus officinalis = 1) were collected directly from beekeepers and analysed for pollen profile, basic physicochemical parameters, antioxidant capacity, radical scavenging activity, total phenolic contents as well as antibacterial properties against pathogenic bacteria Staphylococcus aureus, Escherichia coli, Klebsiella pneumoniae, Salmonella spp. The physicochemical properties of melilot honey were specific for light-coloured unifloral honey samples and were not dependent on its botanical and geographical origin (P > 0·05). All tested honey samples exhibited inhibitory activity (above 90%) against Gram-positive bacteria at the concentration of 12·5-25%. Above 30-50% of antibacterial activity of melilot honey was connected with glucose oxidase enzyme action and was destroyed in the presence of catalase. Hydrogen peroxide-dependent antibacterial activity of honey was inversely correlated with its radical scavenging activity (r = -0·67) and phenolic compounds (r = -0·61). Antibacterial action of melilot honey depends not only on hydrogen peroxide produced by glucose oxidase, but also on other nonperoxide bioactive components of honey. SIGNIFICANCE AND IMPACT OF THE STUDY: Melilot honey is used in traditional medicine as an anticoagulant agent due to the possibility of the presence of the coumarin compounds which are specific for Melilotus plant. Melilotus albus is rarely used to produce honey, and antibacterial properties of this variety of honey had not been studied yet. Nine samples of melilot honey produced in different regions of Poland were analysed according to their antibacterial activity which was correlated with physiochemical parameters and antioxidant activity. It was shown that antibacterial activity of melilot honey is created by hydrogen peroxide and other bioactive compounds.


Subject(s)
Anti-Bacterial Agents/pharmacology , Escherichia coli/drug effects , Honey/analysis , Hydrogen Peroxide/chemistry , Klebsiella pneumoniae/drug effects , Salmonella/drug effects , Staphylococcus aureus/drug effects , Animals , Antioxidants/pharmacology , Beekeeping , Bees/metabolism , Catalase , Melilotus/metabolism , Microbial Sensitivity Tests , Phenols/pharmacology , Plants/chemistry , Poland
2.
Comp Biochem Physiol B Biochem Mol Biol ; 127(3): 383-90, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11126769

ABSTRACT

The goal of this study was to assess the contributions of the most important acid glycosidases to the processes connected with testes involution (in the summer) and spermatogenesis during the reproductive season (the spring) in ganders. Statistically significant increases in the specific activity of N-acetyl-beta-D-hexosaminidase, alpha-D-galactosidase, beta-D-galactosidase, and alpha-L-fucosidase during the period of testes involution were detected. Alpha-D-galactosidase, beta-D-galactosidase, and alpha-D-glucosidase showed an increase in the relative contribution of those multiple forms which are characterized by less acidic values of the pI during the reproductive season. It is suggested that the observed increases in the specific activity of beta-HEX, alpha-GAL, beta-GAL and alpha-FUC may be connected with the catabolism of glycoconjugates, when the spermatogenic activity of the testes declines. The increases in the relative contribution of less acidic forms of alpha-GAL, beta-GAL, and alpha-GLU during the reproductive season may be linked to the rise in the number of spermatocytes, spermatids and spermatozoa during spermatogenesis.


Subject(s)
Geese/metabolism , Glycoside Hydrolases/metabolism , Seasons , Testis/enzymology , Animals , Male , Mannosidases/metabolism , Proteins/metabolism , alpha-Galactosidase/metabolism , alpha-Glucosidases/metabolism , alpha-L-Fucosidase/metabolism , alpha-Mannosidase , beta-Galactosidase/metabolism , beta-Mannosidase , beta-N-Acetylhexosaminidases/metabolism
3.
Folia Biol (Krakow) ; 41(3-4): 49-54, 1993.
Article in English | MEDLINE | ID: mdl-8056087

ABSTRACT

Five multiple forms of alpha-D-mannosidase from turkey seminal plasma were separated by chromatofocusing. The enzyme forms yielded different native M(r) and pI values. Other biochemical properties such as optimum pH, the Km values, thermal stability at 65 degrees C, and the effect of some ionic compounds and carbohydrates on the enzyme activity were similar for all forms.


Subject(s)
Mannosidases/isolation & purification , Semen/enzymology , Animals , Catalysis , Cations, Divalent , Chromatography, Gel , Enzyme Stability , Hydrogen-Ion Concentration , Isoelectric Focusing , Male , Mannosidases/metabolism , Turkeys , alpha-Mannosidase
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