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Production of Transglycosylated Rutin Using Novel Cyclodextrin Glucanotransferase
Corresponding Author(s) : B.L. Pan
Asian Journal of Chemistry,
Vol. 25 No. 9 (2013): Vol 25 Issue 9
Abstract
Besides physical and chemical methods, the enzymatic method could be applied on the modification of rutin molecule. In this study, the transglycosylation of rutin using novel cyclodextrin glucanotransferase (CGTase) produced by Bacillus sp. SK13.002 has been investigated. The optimization of enzymatic reaction conditions using orthogonal experimental design has also been carried out based on temperature, pH, the amount of enzyme cyclodextrin glucanotransferase and the reaction time. The results indicated that among these enzymatic reaction conditions reaction time is the most important variable. Under the optimized enzymatic reaction conditions of pH 5.5, temperature 35 ºC, 20 U cyclodextrin glucanotransferase per mL reaction system and 24 h of reaction time, the transglycosylation conversation rate of rutin could reach as high as 65.7 %. Furthermore the change of the components of transglycosylated rutins during the rutin transglycosylation has also been investigated.
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Q. Huo, X.M. Gu, Q. Lin, Y.J. Sun, C.X. Xu and L. Xiao, Asian J. Chem., 23, 3413 (2011).
M.L. Calabro, S. Tommasini, P. Donato, R. Stancanelli, D. Raneri, S. Catania, C. Costa, V. Villari, P. Ficarra and R. Ficarra, J. Pharm. Biomed. Anal., 36, 1019 (2005).
A. Korkmaz and D. Kolankaya, J. Surg. Res., 164, 309 (2010).
A.R. Verma, M. Vijayakumar, C.S. Mathela and C.V. Rao, Food Chem. Toxicol., 47, 2196 (2009).
S. Itagaki, J. Oikawa, J. Ogura, M. Kobayashi, T. Hirano and K. Iseki, Food Chem., 118, 426 (2010).
R. Mauludin, R.H. Müller and C.M. Keck, Int. J. Pharm., 370, 202 (2009).
R. Mauludin, R.H. Müller and C.M. Keck, Eur. J. Pharm. Sci., 36, 502 (2009).
P. Couvreur, G. Barrat, E. Fattal, P. Legrand and C. Vauthier, Ther. Drug Carrier Syst., 19, 99 (2002).
Y. Suzuki and K. Suzuki, Agric. Biol. Chem., 55, 181 (1991).
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H. Aga, M. Yoneyama, S. Sakai and I. Yamamoto, Agric. Biol. Chem., 55, 1751 (1991).
V. Jaitak, V.K. Kaul, Bandna, N. Kumar, B. Singh, L.S. Savergave, V.V. Jogdand and S. Nene, Biotechnol. Lett., 31, 1415 (2009).
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M. Sato, K. Nakamura, H. Nagano, Y. Yagi and K. Koizumi, Biotechnol. Lett., 14, 654 (1992).
T. Shibuya, Y. Miwa, M. Nakano, T. Yamauchi, H. Chaen, S. Sakai and M. Kurimoto, Biosci. Biotechnol. Biochem., 57, 56 (1993).
T. Kometani, Y. Terada, T. Nishimura, H. Takii and S. Okada, Biosci. Biotechnol. Biochem., 58, 1990 (1994).
S. Riva, J. Mol. Catal. B, 19-20, 43 (2002).
D.G. Yim, H.H. Sato, Y.H. Park and Y.K. Park, J. Ind. Micorbial. Biotechnol., 18, 402 (1997).
N. Charoenlap, S. Dharmsthiti, S. Sirisansaneeyakul and S. Lertsiri, Bioresour. Technol., 92, 49 (2004).
N. Szerman, I. Schroh, A.L. Rossi, A.M. Rosso, N. Krymkiewicz and S.A. Ferrarotti, Bioresour. Technol., 98, 2886 (2007).
B. Zhekova, G. Dobrev, V. Stanchev and I. Pishtiyski, World J. Microbiol. Biotechnol., 25, 1043 (2009).
C.S. Park, K.H. Park and S.H. Kim, Agric. Biol. Chem., 53, 1167 (1989).
T. Sun, B. Jiang and B.L. Pan, Sci. Technol. Food Ind., 9, 358 (2010).
H.B. Wan, W.G. Lan, M.K. Wong and C.Y. Mok, Anal. Chim. Acta, 289, 371 (1994).
L.Q. Yang, P.C. Li and S.J. Fan, Chin. J. Oceanol. Limnol., 26, 193 (2008).
H.J. Chung, S.H. Yoon, M.-J. Lee, M.-J. Kim, K.-S. Kweon, I.-W. Lee, J.-W. Kim, B.-H. Oh, H.-S. Lee, V.A. Spiridonova and K.-H. Park, J. Agric. Food Chem., 46, 952 (1998).
K. Tomita, M. Kaneda and K. Kawamura, J. Ferm. Bioeng., 75, 89 (1993).
Y.H. Go, T.K. Kim, K.W. Lee and Y.H. Lee, J. Microbiol. Biotechnol., 17, 1550 (2007).
S. Jemli, E.B. Messaoud, D. Ayadi-Zouari, B. Naili, B. Khemakhem and S.A. Bejar, Biochem. Eng. J., 34, 44 (2007).
H.A. Alves-Prado, E. Gomes and R. da Silva, Appl. Biochem. Biotechnol., 136-140, 41 (2007).
B.N. Gawande and A.Y. Patkar, Enzym. Microbiol. Technol., 28, 735 (2001).
T. Sun, B. Jiang and B.L. Pan, Int. J. Mol. Sci., 11, 3786 (2011).
A.M. Klibanov, Chem. Technol., 6, 354 (1986).