scholarly journals New Insights Into Cinnamoyl Esterase Activity of Oenococcus oeni

2019 ◽  
Vol 10 ◽  
Author(s):  
Ingrid Collombel ◽  
Chrats Melkonian ◽  
Douwe Molenaar ◽  
Francisco M. Campos ◽  
Tim Hogg
Keyword(s):  
Esterase Activity ◽  
Oenococcus Oeni ◽  
Cinnamoyl Esterase

scholarly journals Influence ofOenococcus oeniandBrettanomyces bruxellensison Aged Wine Microbial Taxonomic and Functional Profiles

2017 ◽  
Author(s):  
Marie Lisandra Zepeda-Mendoza ◽  
Nathalia Kruse Edwards ◽  
Mikkel Gulmann Madsen ◽  
Martin Abel-Kistrup ◽  
Lara Puetz ◽  
...  
Keyword(s):  
Microbial Community ◽  
Esterase Activity ◽  
Oenococcus Oeni ◽  
Flavor Compounds ◽  
Microbial Inoculants ◽  
Wine Quality ◽  
Brettanomyces Bruxellensis ◽  
Spoilage Yeast ◽  
Cinnamoyl Esterase ◽  
Functional Profiles

AbstractIn the wine making process, the interactions between lactic acid bacteria (LAB), yeast and other wine microflora have an impact on the wine quality. In this study, we investigate the influence of the LABOenococcus oeniand the spoilage yeastBrettanomyces bruxellensison the microbial community of a Cabernet Sauvignon wine. We generated metagenomic datasets from inoculations of three strains ofB. bruxellensis, in combination with twoO. oenistrains, one with and one without cinnamoyl esterase activity. This esterase activity releases hydroxycinnamic acids (HCAs) that can subsequently be processed by someB. bruxellensisstrains able to generate off-flavor compounds. We evaluated the influence of theO. oeniandB. bruxellensison the microbial taxonomic and functional potential profile, particularly regarding off-flavor formation due to HCAs. We found that the effect on the microbial profiles depends oni) theO. oeniandB. bruxellensisstrains being combined andii) the abundance they reach in the final wine, which depends on certain unidentified conditions. We confirmed that the potential ofB. bruxellensisto produce off-flavor compounds from HCAs depends on the strain. Interestingly, the samples without microbial inoculants also had this potential, suggesting that native grape microbiota could also influence the levels of HCA. We also found that the presence ofB. bruxellensisdoes not interfere with the malolactic fermentation of the evaluatedO. oenistrains, which leads to a less acidic taste. We show that metagenomic approaches can help uncover the complex wine microbial community traits, such as flavor, impacted by the simultaneous presence ofO. oeniandB. bruxellensis.

Isolation and characterization of a Clostridium sp. with cinnamoyl esterase activity and unusual cell envelope ultrastructure

1999 ◽  
Vol 172 (3) ◽  
pp. 139-149 ◽  
Author(s):  
C. S. McSweeney ◽  
Amanda Dulieu ◽  
Richard I. Webb ◽  
Therese Del Dot ◽  
Linda L. Blackall
Keyword(s):  
Esterase Activity ◽  
Cell Envelope ◽  
Isolation And Characterization ◽  
Cinnamoyl Esterase

Butyrivibriospp. and Other Xylanolytic Microorganisms From the Rumen have Cinnamoyl Esterase Activity

Anaerobe ◽  
1998 ◽  
Vol 4 (1) ◽  
pp. 57-65 ◽  
Author(s):  
C.S. McSweeney ◽  
A. Dulieu ◽  
R. Bunch
Keyword(s):  
Esterase Activity ◽  
Cinnamoyl Esterase

Beta-glucosidase and esterase activity from Oenococcus oeni: Screening and evaluation during malolactic fermentation in harsh conditions

LWT ◽  
2018 ◽  
Vol 89 ◽  
pp. 262-268 ◽  
Author(s):  
Giovanna Fia ◽  
Valentina Millarini ◽  
Lisa Granchi ◽  
Ginevra Bucalossi ◽  
Simona Guerrini ◽  
...  
Keyword(s):  
Esterase Activity ◽  
Malolactic Fermentation ◽  
Oenococcus Oeni ◽  
Beta Glucosidase ◽  
Harsh Conditions

scholarly journals An enzyme from Auricularia auricula-judae combining both benzoyl and cinnamoyl esterase activity

2013 ◽  
Vol 48 (12) ◽  
pp. 1872-1878 ◽  
Author(s):  
Paul Haase-Aschoff ◽  
Diana Linke ◽  
Manfred Nimtz ◽  
Lutz Popper ◽  
Ralf G. Berger
Keyword(s):  
Esterase Activity ◽  
Auricularia Auricula ◽  
Cinnamoyl Esterase

scholarly journals Bacterial Cinnamoyl Esterase Activity Screening for the Production of a Novel Functional Food Product

2007 ◽  
Vol 74 (4) ◽  
pp. 1284-1288 ◽  
Author(s):  
Simone Guglielmetti ◽  
Ivano De Noni ◽  
Federica Caracciolo ◽  
Francesco Molinari ◽  
Carlo Parini ◽  
...  
Keyword(s):  
Esterase Activity ◽  
Food Product ◽  
Lactobacillus Helveticus ◽  
Probiotic Properties ◽  
The Novel ◽  
High Concentration ◽  
Antioxidant Power ◽  
Cinnamoyl Esterase ◽  
Total Antioxidant ◽  
Activity Screening

ABSTRACT Lactobacillus helveticus MIMLh5 was selected for its strong cinnamoyl esterase activity on chlorogenic acid and employed for the preparation of a food product containing a high concentration of free caffeic acid. The novel food product was demonstrated to display high total antioxidant power and potential probiotic properties.

Study of Thrombin-Coagulase

1967 ◽  
Vol 17 (03/04) ◽  
pp. 321-334 ◽  
Author(s):  
J. P Soulier ◽  
Odette Prou-Wartelle ◽  
Liliane Hallé ◽  
Keyword(s):  
Esterase Activity ◽  
Adsorption Chromatography ◽  
The Difference

SummaryThe preparation of thrombin-coagulase is described. The properties of thrombin-coagulase are compared with those of biothrombin: kinetics, thermostability, adsorption, chromatography, esterase activity, clotting activity, action on platelets and on factors V and VIII, susceptibility to inhibitors.Biothrombin and thrombin-coagulase are closely related but distinct. Both apparently derive from prothrombin. Prothrombin and coagulase combine to form a complex: thrombin-coagulase wherein both factors are necessary for its activity. Possible explanations for the difference between thrombin-coagulase and biothrombin are proposed.

Activity of Plasmin and Streptokinase-Activator on Substituted Arginine and Lysine Esters

1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher
Keyword(s):  
Molecular Structure ◽  
Methyl Ester ◽  
Comparative Studies ◽  
Esterase Activity ◽  
Methyl Esters ◽  
Hydrolytic Activity ◽  
The Other ◽  
Other Hand

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.

Sign in / Sign up

Export Citation Format

Share Document