Speciality Chemicals Magazine MAR / APR 2021 | Page 49

BIOBASED CHEMICALS acids ( Gln265 , Thr436 , Asn438 and His 442 ), which supposedly mediate carboxylate binding . 18 Up to 18-fold improvement in the conversion of OA derivatives is observed , while highly R-selective hydration ( ee > 95 %) is maintained for all tested substrates . The triple

alanine variant Gln265Ala / Thr436Ala / Asn438Ala has shown the best improvements . 21 Some double and triple EmOhyA variants enable the hydration of sterically demanding oleic acid isopropyl and butyl esters , whereas EmOhyA wild-type fails on these substrates .
Work on FAHYs and OHYs will focus on extending the portfolio of enzymes and on expanding their substrate scope . Ultimately , C = C bonds anywhere in aliphatic substrates will be hydrated regio- and stereoselectively , independent of their position and of the presence of a carboxylate head group .
Conclusions
Hydratases are attractive biocatalysts that can oxyfunctionalise compounds harbouring activated and non-activated C = C bonds in highly regio- and stereoselective manners . 3D structures and reaction mechanisms of hydratases of bacterial and fungal origin have been elucidated , enabling enzyme engineering and substrate scope expansion . Several industrial processes are established that employ hydratases either as isolated enzymes or in whole-cell approaches . The discovery of novel hydratases and the evolution of known hydratases will pave the way to green , sustainable processes based on renewable natural feedstocks . •
Figure 4 – Structure-based exchange of amino acid residues enhances conversion of non-natural oleate hydratase substrates
Dr Martin Trinker
DIRECTOR BUSINESS DEVELOPMENT & FUNDRAISING
ACIB GMBH k + 43 316 873 9316 J martin . trinker @ acib . at j www . acib . at
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