Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis
Само за регистроване кориснике
2012
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be a-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate.
Кључне речи:
transglucosylation kinetic / maltase / vanillyl alcohol / substrate inhibition / vanillyl alcohol isomaltosideИзвор:
Biotechnology Progress, 2012, 28, 6, 1450-1456Издавач:
- Wiley, Hoboken
Финансирање / пројекти:
- 451-03-00605/2012-16/51
- Алергени, антитела, ензими и мали физиолошки значајни молекули: дизајн, структура, функција и значај (RS-MESTD-Basic Research (BR or ON)-172049)
- Развој нових инкапсулационих и ензимских технологија за производњу биокатализатора и биолошки активних компонената хране у циљу повећања њене конкурентности, квалитета и безбедности (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
DOI: 10.1002/btpr.1628
ISSN: 8756-7938
PubMed: 22927369
WoS: 000312157100008
Scopus: 2-s2.0-84872404655
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Dimitrijević, Aleksandra AU - Veličković, Dušan AU - Milosavić, Nenad AU - Bezbradica, Dejan PY - 2012 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2157 AB - Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be a-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate. PB - Wiley, Hoboken T2 - Biotechnology Progress T1 - Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis EP - 1456 IS - 6 SP - 1450 VL - 28 DO - 10.1002/btpr.1628 ER -
@article{ author = "Dimitrijević, Aleksandra and Veličković, Dušan and Milosavić, Nenad and Bezbradica, Dejan", year = "2012", abstract = "Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be a-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate.", publisher = "Wiley, Hoboken", journal = "Biotechnology Progress", title = "Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis", pages = "1456-1450", number = "6", volume = "28", doi = "10.1002/btpr.1628" }
Dimitrijević, A., Veličković, D., Milosavić, N.,& Bezbradica, D.. (2012). Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. in Biotechnology Progress Wiley, Hoboken., 28(6), 1450-1456. https://doi.org/10.1002/btpr.1628
Dimitrijević A, Veličković D, Milosavić N, Bezbradica D. Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. in Biotechnology Progress. 2012;28(6):1450-1456. doi:10.1002/btpr.1628 .
Dimitrijević, Aleksandra, Veličković, Dušan, Milosavić, Nenad, Bezbradica, Dejan, "Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis" in Biotechnology Progress, 28, no. 6 (2012):1450-1456, https://doi.org/10.1002/btpr.1628 . .