Title of article
On the inactivity of Candida antartica lipase B towards strong acids
Author/Authors
Hollmann، نويسنده , , F. and Grzebyk، نويسنده , , P. and Heinrichs، نويسنده , , V. and Doderer، نويسنده , , K. and Thum، نويسنده , , O.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2009
Pages
5
From page
257
To page
261
Abstract
Candida antarctica lipase B (CalB, Novozyme 435) was evaluated as catalyst for the conversion of so-called edible acids (e.g. malic and tartaric acid). While transesterification using these acyl donors proceeds smoothly, albeit with low regioselectivity, esterification is hardly catalyzed.
or reason for CalB inactivation the high acidity of edible acids was identified leading to irreversible inactivation of the biocatalyst. Furthermore, indication exist that all acids exhibiting a pKa value below 4.8 cause irreversible inactivation of CalB.
Keywords
enzyme catalysis , Enzyme inactivation , Esterification , Lipases
Journal title
Journal of Molecular Catalysis B Enzymatic
Serial Year
2009
Journal title
Journal of Molecular Catalysis B Enzymatic
Record number
1713749
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