Efficient enzymatic synthesis of amide with (aminomethyl)trimethylsilane

Abstract

Hydrolase-catalyzed amide synthesis using a silicon-containing amine, (aminomethyl)trimethylsilane, as the substrate was studied. Six hydrolases (lipase OF 360, lipase Novo, lipase KLIP-001, lipoprotein lipase Type A, cholesterol esterase Type A, and cholesterol esterase III) were capable of forming the amide of (aminomethyl)trimethylsilane with octanoic acid in 2,2,4-trimethylpentane. Lipoprotein lipase Type A and cholesterol esterase Type A showed particularly the high levels of activity. From a comparative study of (aminomethyl)trimethylsilane and its carbon analog, 2,2- dimethylpropylamine, the former was found to be a better substrate for the hydrolases than the carbon analog. This difference is considered to arise from the specific properties of the silicon atom. (Aminomethyl)trimethylsilane exhibited a homotropic effect at concentration under 100 mM in amide synthesis by lipoprotein lipase Type A, while the carbon analog showed no such effect.

Source or Periodical Title

Journal of Bioscience and Bioengineering

ISSN

13891723

Page

607-610

Document Type

Article

Subject

(aminomethyl)trimethylsilane, 2, 2- dimethylpropylamine, Amide formation, Hydrolase, Silicon-containing amine

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