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Lipase-catalyzed synthesis and characterization of myristoyl maltose ester

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Abstract

Myristoyl maltose ester was synthesized by lipase-catalyzed reaction of maltose and myristic acid. Influence of different reaction parameters, such as molecular sieve concentration, molar ratio of acid/sugar, enzyme concentration, reaction time, and reaction temperature, was studied. Under the optimum conditions of 20 g/L molecular sieve, 14% (w/w) lipase from Novozym 435, and acid/sugar molar ratio of 5:1 at 60 °C for 60 h, the highest conversion (90%) was achieved. The as-prepared maltose ester was confirmed by Fourier-transform infrared spectra (FTIR), liquid chromatograph–mass spectrum (LC–MS), and scanning electron microscopy (SEM).

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Acknowledgments

This work is financially supported by National 863 Project grant (No. 2007AA100401).

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Correspondence to Ping Sun.

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Sun, P., Chen, Y., Wang, H. et al. Lipase-catalyzed synthesis and characterization of myristoyl maltose ester. Eur Food Res Technol 233, 253–258 (2011). https://doi.org/10.1007/s00217-011-1490-0

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  • DOI: https://doi.org/10.1007/s00217-011-1490-0

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