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Volume 6, Issue 8 (Suppl) J Biotechnol Biomater
ISSN: 2155-952X JBTBM, an open access journal Bio America 2016
November 28-30, 2016
November 28-30, 2016 San Francisco, USA
13th Biotechnology Congress
Shota Kajiwara et al., J Biotechnol Biomater 2016, 6:8(Suppl)
Development of lipase-sucrose complex to improve of transesterification activity and stability in the organic
solvents
Shota Kajiwara, Ryosuke Yamada and Hiroyasu Ogino
Osaka Prefecture University, Japan
Lipases are one of the most important enzymes as industrial catalysts. When lipases are used in the presence of organic solvents,
the reaction rate is remarkably increased by solubilizing the poorly soluble substrates. Furthermore, lipases can catalyze ester
synthetic reactions and transesterification reactions in the presence of organic solvents. However, enzymes including lipases are
generally inactivated in the presence of organic solvents by direct contact with molecules of organic solvents. Some coordinated water
molecules exist around sugars such as sucrose. Thus when lipase was complexed with sucrose and used in the presence of organic
solvents, coordinated water molecules around the lipase-sucrose complex might reduce direct contact between lipase and organic
solvent molecules. In this study, the transesterification activity of the lipase-sucrose complex in the presence of organic solvents was
examined. The lipase-sucrose complex was prepared by freeze-dry of a lipase solution containing 1% (w/v) of sucrose (mass ratio of
Lipase & Sucrose is 1:130). The lipase-sucrose complex showed the higher transesterification activity than freeze-dried lipase without
sucrose in the presence of n-hexane and n-hexane containing 50% (v/v) of n-octane, 1-propanol, 1-pentanol, or 1-octanol. After
incubation in 100% of n-hexane, n-octane or 1-propanol at 30 oC for 24 hours, the residual transesterification activity of lipase-
sucrose complex was higher than that of the freeze-dried lipase without sucrose. Furthermore, after incubation in 100% of 1-pentanol
or 1-octanol, the transesterification activity of lipase-sucrose complex was also increased. In conclusion, the transesterification
activity and organic solvent-stability of the lipase were successfully improved by complexation with sucrose.
Biography
Shota Kajiwara has received his Master of Engineering degree in Osaka Prefecture University, Osaka, Japan in 2016. He is currently a Doctoral student of Osaka
Prefecture University. His research interest includes the stabilization of enzyme in the presence of organic solvents.