Improved Recovery of an Ester Flavor Compound by Pervaporation Coupled with a Flash Condensation

1999 ◽  
Vol 38 (11) ◽  
pp. 4458-4469 ◽  
Author(s):  
Arnaud Baudot ◽  
Michèle Marin
Keyword(s):  
Author(s):  
Aileen Becker ◽  
Dominique Böttcher ◽  
Werner Katzer ◽  
Karsten Siems ◽  
Lutz Müller-Kuhrt ◽  
...  

Abstract Raspberry ketone is a widely used flavor compound in food and cosmetic industry. Several processes for its biocatalytic production have already been described, but either with the use of genetically modified organisms (GMOs) or incomplete conversion of the variety of precursors that are available in nature. Such natural precursors are rhododendrol glycosides with different proportions of (R)- and (S)-rhododendrol depending on the origin. After hydrolysis of these rhododendrol glycosides, the formed rhododendrol enantiomers have to be oxidized to obtain the final product raspberry ketone. To be able to achieve a high conversion with different starting material, we assembled an alcohol dehydrogenase toolbox that can be accessed depending on the optical purity of the intermediate rhododendrol. This is demonstrated by converting racemic rhododendrol using a combination of (R)- and (S)-selective alcohol dehydrogenases together with a universal cofactor recycling system. Furthermore, we conducted a biocatalytic cascade reaction starting from naturally derived rhododendrol glycosides by the use of a glucosidase and an alcohol dehydrogenase to produce raspberry ketone in high yield. Key points • LB-ADH, LK-ADH and LS-ADH oxidize (R)-rhododendrol • RR-ADH and ADH1E oxidize (S)-rhododendrol • Raspberry ketone production via glucosidase and alcohol dehydrogenases from a toolbox Graphical abstract


2014 ◽  
pp. 493-498
Author(s):  
Elisabeth Guichard ◽  
Claude Yven ◽  
Marie Repoux ◽  
Etienne Sémon ◽  
Hélène Labouré ◽  
...  

2013 ◽  
Vol 85-86 ◽  
pp. 93-98 ◽  
Author(s):  
Olga Bortolini ◽  
Pier Paolo Giovannini ◽  
Silvia Maietti ◽  
Alessandro Massi ◽  
Paola Pedrini ◽  
...  

Author(s):  
WS Schlotzhauer ◽  
RF Severson ◽  
RM Martin

AbstractSucrose esters, principally the 6-O-acetyl-2,3,4-tri-O-(3-methylvaleryl)-a-D-glucopyranosyl-b-D-fructofuran-oside isomer, isolated from the cuticular waxes of green T.I. 165 tobacco leaf, were evaluated as enhancers of 3-methylvaleric acid in the smoke of a tobacco deficient in this important flavor compound. Analyses of the products from semi-micro pyrolyses of sucrose and isolated sucrose esters, over a temperature range of 250°C - 850°C, showed that free sucrose produced 5-hydroxy-methylfurfural as the major component, whereas the ester isolate yielded 3-methylvaleric acid and lesser amounts of isomeric C4 and C5 aliphatic acids. Incorporation of sucrose ester isolate of T.I. 165 leaf into cigarettes prepared from flue-cured NC 2326 tobacco, the smoke of which is essentially devoid of 3-methylvaleric acid, resulted in a total particulate matter with enhanced levels of this compound. The data indicated that addition of approximately 2 mg of sucrose ester isolate per cigarette produced levels of 3-methylvaleric acid in the smoke of NC 2326 cigarettes that were comparable to levels observed in the smoke from cigarettes containing all T.I. 165 or blended Turkish tobacco.


2011 ◽  
Vol 94 (3) ◽  
pp. 923-930 ◽  
Author(s):  
Koichi Saito ◽  
Kouhei Hosono ◽  
Nariko Kitazawa ◽  
Yusuke Iwasaki ◽  
Rie Ito ◽  
...  

Abstract A quality assessment method for commercially available, optically active flavor compounds, namely, menthol, menthyl acetate, borneol, perillaldehyde, and 1,8-cineol, was developed. A gas chromatograph equipped with a flame ionization detector and a DB-5ms capillary column was used for the chemical purity test. A GC/MS with a β-DEX cyclodextrin column was used for the optical purity test, by which the enantiomeric separation of each flavor compound was achieved. Enantiomeric excess was calculated as an expression of optical purity. Of the 25 standard samples subjected to the chemical purity test, six were found to have lower purity than the data provided by the manufacturers. When the same samples were subjected to the optical purity test, 11 were found to have lower purity than that indicated on the reagent labels. These results suggest that there is a need to conduct an optical purity test, in addition to a chemical purity test, for the quality assessment of flavor standards.


2020 ◽  
Vol 104 (21) ◽  
pp. 9205-9218
Author(s):  
Nina Jankowski ◽  
Katja Koschorreck ◽  
Vlada B. Urlacher

Abstract The fungal secretome comprises various oxidative enzymes participating in the degradation of lignocellulosic biomass as a central step in carbon recycling. Among the secreted enzymes, aryl-alcohol oxidases (AAOs) are of interest for biotechnological applications including production of bio-based precursors for plastics, bioactive compounds, and flavors and fragrances. Aryl-alcohol oxidase 2 (PeAAO2) from the fungus Pleurotus eryngii was heterologously expressed and secreted at one of the highest yields reported so far of 315 mg/l using the methylotrophic yeast Pichia pastoris (recently reclassified as Komagataella phaffii). The glycosylated PeAAO2 exhibited a high stability in a broad pH range between pH 3.0 and 9.0 and high thermal stability up to 55 °C. Substrate screening with 41 compounds revealed that PeAAO2 oxidized typical AAO substrates like p-anisyl alcohol, veratryl alcohol, and trans,trans-2,4-hexadienol with up to 8-fold higher activity than benzyl alcohol. Several compounds not yet reported as substrates for AAOs were oxidized by PeAAO2 as well. Among them, cumic alcohol and piperonyl alcohol were oxidized to cuminaldehyde and piperonal with high catalytic efficiencies of 84.1 and 600.2 mM−1 s−1, respectively. While the fragrance and flavor compound piperonal also serves as starting material for agrochemical and pharmaceutical building blocks, various positive health effects have been attributed to cuminaldehyde including anticancer, antidiabetic, and neuroprotective effects. PeAAO2 is thus a promising biocatalyst for biotechnological applications. Key points • Aryl-alcohol oxidase PeAAO2 from P. eryngii was produced in P. pastoris at 315 mg/l. • Purified enzyme exhibited stability over a broad pH and temperature range. • Oxidation products cuminaldehyde and piperonal are of biotechnological interest. Graphical abstract


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