Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 362-365 |
| Seitenumfang | 4 |
| Fachzeitschrift | Flavour and fragrance journal |
| Jahrgang | 30 |
| Ausgabenummer | 5 |
| Publikationsstatus | Veröffentlicht - 12 Mai 2015 |
Abstract
Dehydrodivanillin, the symmetrical dimer of vanillin, is a taste enhancer which imparts pleasant impressions of creaminess to food. Found in vanilla pods in traces only, a co-substrate independent dimerization of vanillin, conducted in a co-solvent system to improve the solubility of vanillin, was developed using iso-active fungal laccases from Meripilus giganteus, Agaricus bisporus and Funalia trogii. The yields were compared with a peroxidase from Marasmius scorodonius (MsP2) and the reference enzyme horseradish peroxidase (HRP), both supplied with hydrogen peroxide. Using laccase catalysis, the kinetically preferred reaction product, 5,5'-dehydrodivanillin, rapidly reached saturation and precipitated in situ, thus shifting the reaction equilibrium to the product. Yields of>95 % were obtained with the high-redox-potential laccase of Funalia trogii, while HRP gave 18 %.
ASJC Scopus Sachgebiete
- Agrar- und Biowissenschaften (insg.)
- Lebensmittelwissenschaften
- Chemie (insg.)
- Allgemeine Chemie
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in: Flavour and fragrance journal, Jahrgang 30, Nr. 5, 12.05.2015, S. 362-365.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung
}
TY - JOUR
T1 - The taste enhancer divanillin
T2 - A review on sources and enzymatic generation
AU - Krings, Ulrich
AU - Esparan, Vida
AU - Berger, Ralf G.
PY - 2015/5/12
Y1 - 2015/5/12
N2 - Dehydrodivanillin, the symmetrical dimer of vanillin, is a taste enhancer which imparts pleasant impressions of creaminess to food. Found in vanilla pods in traces only, a co-substrate independent dimerization of vanillin, conducted in a co-solvent system to improve the solubility of vanillin, was developed using iso-active fungal laccases from Meripilus giganteus, Agaricus bisporus and Funalia trogii. The yields were compared with a peroxidase from Marasmius scorodonius (MsP2) and the reference enzyme horseradish peroxidase (HRP), both supplied with hydrogen peroxide. Using laccase catalysis, the kinetically preferred reaction product, 5,5'-dehydrodivanillin, rapidly reached saturation and precipitated in situ, thus shifting the reaction equilibrium to the product. Yields of>95 % were obtained with the high-redox-potential laccase of Funalia trogii, while HRP gave 18 %.
AB - Dehydrodivanillin, the symmetrical dimer of vanillin, is a taste enhancer which imparts pleasant impressions of creaminess to food. Found in vanilla pods in traces only, a co-substrate independent dimerization of vanillin, conducted in a co-solvent system to improve the solubility of vanillin, was developed using iso-active fungal laccases from Meripilus giganteus, Agaricus bisporus and Funalia trogii. The yields were compared with a peroxidase from Marasmius scorodonius (MsP2) and the reference enzyme horseradish peroxidase (HRP), both supplied with hydrogen peroxide. Using laccase catalysis, the kinetically preferred reaction product, 5,5'-dehydrodivanillin, rapidly reached saturation and precipitated in situ, thus shifting the reaction equilibrium to the product. Yields of>95 % were obtained with the high-redox-potential laccase of Funalia trogii, while HRP gave 18 %.
KW - Co-solvent
KW - Dehydrodivanillin
KW - Laccase
KW - Peroxidase
KW - Reaction equilibrium
KW - Vanillin
UR - http://www.scopus.com/inward/record.url?scp=84938984313&partnerID=8YFLogxK
U2 - 10.1002/ffj.3251
DO - 10.1002/ffj.3251
M3 - Article
AN - SCOPUS:84938984313
VL - 30
SP - 362
EP - 365
JO - Flavour and fragrance journal
JF - Flavour and fragrance journal
SN - 0882-5734
IS - 5
ER -