Abstract
Significance
Hydroxynitrile lyase (HNL) has been isolated from plants and bacteria and is a valuable tool in the chiral-specific synthesis of cyanohydrins, which are important building blocks of fine chemicals and pharmaceuticals. To discover more efficient and stable HNLs, we focused on the invasive cyanogenic millipede as a bioresource. The HNL identified from the millipede showed not only the highest specific activity toward benzaldehyde among known HNLs, including the almond HNL in industrial use, along with wide temperature and pH stabilities, but also high enantioselectivity in the synthesis of various cyanohydrins. These properties make it suitable as an industrial biocatalyst. Arthropods are likely to be valuable sources of potential biocatalysts for the next generation of industrial biotechnology.
Abstract
Hydroxynitrile lyase (HNL) catalyzes the degradation of cyanohydrins and causes the release of hydrogen cyanide (cyanogenesis). HNL can enantioselectively produce cyanohydrins, which are valuable building blocks for the synthesis of fine chemicals and pharmaceuticals, and is used as an important biocatalyst in industrial biotechnology. Currently, HNLs are isolated from plants and bacteria. Because industrial biotechnology requires more efficient and stable enzymes for sustainable development, we must continuously explore other potential enzyme sources for the desired HNLs. Despite the abundance of cyanogenic millipedes in the world, there has been no precise study of the HNLs from these arthropods. Here we report the isolation of HNL from the cyanide-emitting invasive millipede Chamberlinius hualienensis, along with its molecular properties and application in biocatalysis. The purified enzyme displays a very high specific activity in the synthesis of mandelonitrile. It is a glycosylated homodimer protein and shows no apparent sequence identity or homology with proteins in the known databases. It shows biocatalytic activity for the condensation of various aromatic aldehydes with potassium cyanide to produce cyanohydrins and has high stability over a wide range of temperatures and pH values. It catalyzes the synthesis of (R)-mandelonitrile from benzaldehyde with a 99% enantiomeric excess, without using any organic solvents. Arthropod fauna comprise 80% of terrestrial animals. We propose that these animals can be valuable resources for exploring not only HNLs but also diverse, efficient, and stable biocatalysts in industrial biotechnology.
Hydroxynitrile lyase (HNL) has been isolated from plants and bacteria and is a valuable tool in the chiral-specific synthesis of cyanohydrins, which are important building blocks of fine chemicals and pharmaceuticals. To discover more efficient and stable HNLs, we focused on the invasive cyanogenic millipede as a bioresource. The HNL identified from the millipede showed not only the highest specific activity toward benzaldehyde among known HNLs, including the almond HNL in industrial use, along with wide temperature and pH stabilities, but also high enantioselectivity in the synthesis of various cyanohydrins. These properties make it suitable as an industrial biocatalyst. Arthropods are likely to be valuable sources of potential biocatalysts for the next generation of industrial biotechnology.
Abstract
Hydroxynitrile lyase (HNL) catalyzes the degradation of cyanohydrins and causes the release of hydrogen cyanide (cyanogenesis). HNL can enantioselectively produce cyanohydrins, which are valuable building blocks for the synthesis of fine chemicals and pharmaceuticals, and is used as an important biocatalyst in industrial biotechnology. Currently, HNLs are isolated from plants and bacteria. Because industrial biotechnology requires more efficient and stable enzymes for sustainable development, we must continuously explore other potential enzyme sources for the desired HNLs. Despite the abundance of cyanogenic millipedes in the world, there has been no precise study of the HNLs from these arthropods. Here we report the isolation of HNL from the cyanide-emitting invasive millipede Chamberlinius hualienensis, along with its molecular properties and application in biocatalysis. The purified enzyme displays a very high specific activity in the synthesis of mandelonitrile. It is a glycosylated homodimer protein and shows no apparent sequence identity or homology with proteins in the known databases. It shows biocatalytic activity for the condensation of various aromatic aldehydes with potassium cyanide to produce cyanohydrins and has high stability over a wide range of temperatures and pH values. It catalyzes the synthesis of (R)-mandelonitrile from benzaldehyde with a 99% enantiomeric excess, without using any organic solvents. Arthropod fauna comprise 80% of terrestrial animals. We propose that these animals can be valuable resources for exploring not only HNLs but also diverse, efficient, and stable biocatalysts in industrial biotechnology.
| Original language | English |
|---|---|
| Pages (from-to) | 10605-10610 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 112 |
| Issue number | 34 |
| DOIs | |
| Publication status | Published - 10 Aug 2015 |