Preparation and characterization of fermented dandelion (Taraxacum officinale) beverage using Lactobacillus acidophilus F46 having cinnamoyl esterase activity

2015 ◽  
Vol 24 (2) ◽  
pp. 583-593 ◽  
Author(s):  
Jong-Hui Kim ◽  
Sang-Ho Baik
1999 ◽  
Vol 172 (3) ◽  
pp. 139-149 ◽  
Author(s):  
C. S. McSweeney ◽  
Amanda Dulieu ◽  
Richard I. Webb ◽  
Therese Del Dot ◽  
Linda L. Blackall

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
J Kim ◽  
G Choi ◽  
H Hwang ◽  
H Ku ◽  
C Choi ◽  
...  
Keyword(s):  

1998 ◽  
Vol 84 (4) ◽  
pp. 593-599 ◽  
Author(s):  
A. Banina ◽  
M. Vukasinovic ◽  
S. Brankovic ◽  
D. Fira ◽  
M. Kojic ◽  
...  

1979 ◽  
Vol 34 (9-10) ◽  
pp. 715-720 ◽  
Author(s):  
Gerhild Nurmann ◽  
Dieter Strack

Abstract From cotyledons of Raphanus sativus (red radish) an esterase activity which catalyzes the hy­drolysis of sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optimum of 8.5 and the apparent Km is 1.95 × 10-5 m. The enzyme is relatively insensi­tive to both physostigmine (eserine) {Ki = 1.73 × 10-4 m) and neostigmine (Ki = 2 .1 3 × 10-4 ᴍ). Diisopropyl fluorophosphate (DFP) showed no inhibition and diethyl p-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10-5 ᴍ, respectively. Choline (10-2 ᴍ) was inhibitory but acetylcholine (10-2 ᴍ) stimulated the enzyme activity.


Author(s):  
Juliane Zimmerling ◽  
Michel Oelschlägel ◽  
Carolin Großmann ◽  
Matthias Voitel ◽  
Michael Schlömann ◽  
...  

Abstract Four phenylacetaldehyde dehydrogenases (designated as FeaB or StyD) originating from styrene-degrading soil bacteria were biochemically investigated. In this study, we focused on the Michaelis-Menten kinetics towards the presumed native substrate phenylacetaldehyde and the obviously preferred co-substrate NAD+. Furthermore, the substrate specificity on four substituted phenylacetaldehydes and the co-substrate preference were studied. Moreover, these enzymes were characterized with respect to their temperature as well as long-term stability. Since aldehyde dehydrogenases are known to show often dehydrogenase as well as esterase activity, we tested this capacity, too. Almost all results showed clearly different characteristics between the FeaB and StyD enzymes. Furthermore, FeaB from Sphingopyxis fribergensis Kp5.2 turned out to be the most active enzyme with an apparent specific activity of 17.8 ± 2.1 U mg-1. Compared with that, both StyDs showed only activities less than 0.2 U mg-1 except the overwhelming esterase activity of StyD-CWB2 (1.4 ± 0.1 U mg-1). The clustering of both FeaB and StyD enzymes with respect to their characteristics could also be mirrored in the phylogenetic analysis of twelve dehydrogenases originating from different soil bacteria.


1977 ◽  
Vol 40 (9) ◽  
pp. 614-616 ◽  
Author(s):  
A. GAVIN ◽  
K. OSTOVAR

Milk samples of five breast-feeding mothers were studied for bacterial population, flora, and source. In most instances, samples taken at postfeeding contained higher bacterial populations than prefeeding samples. Staphylococcus epidermidis was the predominant organism isolated from 100% of the samples. Increases were noticed in the appearance of Streptococcus mitis, Gaffkya tetragena, Streptococcus salivarius, Staphylococcus aureus, as well as Lactobacillus acidophilus, in the postfeeding samples. Main sources of bacteria were found to be the infant's mouth and maternal skin.


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