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. 2018 Oct;82(10):1760-1769.
doi: 10.1080/09168451.2018.1490171. Epub 2018 Jul 5.

Characterization of a novel hydroxynitrile lyase from Nandina domestica Thunb

Kimiyasu Isobe  1   2 , Asuka Kitagawa  1 , Kazuma Kanamori  1 , Nozomi Kashiwagi  1 , Daisuke Matsui  1   2 , Takuya Yamaguchi  2 , Ken-Ichi Fuhshuku  1 , Hisashi Semba  3 , Yasuhisa Asano  1   2
Affiliations

Characterization of a novel hydroxynitrile lyase from Nandina domestica Thunb

Kimiyasu Isobe et al. Biosci Biotechnol Biochem. 2018 Oct.

Abstract

The leaves of Nandina domestica Thunb. exhibited high hydroxynitrile lyase (HNL) activity in (R)-mandelonitrile synthesis. The specific activity of young leaves was significantly higher than that of mature leaves. We isolated two HNLs with molecular mass of 24.9 kDa (NdHNL-S) and 28.0 kDa (NdHNL-L) from the young leaves. Both NdHNLs were composed of two identical subunits, without FAD and carbohydrates. We purified NdHNL-L and revealed its enzymatic properties. The whole deduced amino acid sequence of NdHNL-L was not homologous to any other HNLs, and the specific activity for mandelonitrile synthesis by NdHNL-L was higher than that by other plant HNLs. The enzyme catalyzed enantioselective synthesis of (R)-cyanohydrins, exhibited high activity at pH 4.0, and high stability in the pH range of 3.5-8.0 and below 55°C. Thus, NdHNL-L is a novel HNL with novel amino acid sequence and has a potential for the efficient production of (R)-cyanohydrins.

Keywords: Hydroxynitrile lyase; Nandina domestica; benzaldehyde; cyanohydrin; mandelonitrile.

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