By Bo Mattiasson, Lei Ye
Managed radical polymerization options for molecular imprinting, through Mark E. Byrne
From bulk polymers to nanoparticles, via Lei Ye
Post-imprinting and in-cavity functionalization, via Toshifumi Takeuchi
Characterization of MIPs (affinity, selectivity, web site heterogeneity…), by means of Richard Ansell
Theoretical elements and machine modelling, by way of Ian Nicholls
MIPs in aqueous environments, by way of Bin Lu
MIPs for binding macromolecules, via Kenneth J. Shea
Solid part extraction, by way of Ecevit Yilmaz
Sensors, by way of Sergey A. Piletsky
MIPs for catalysis and synthesis, by means of Marina Resmini
Wastewater therapy, via Bo Mattiasson
MIPs as instruments for bioassays, biotransformation and drug supply, through Meiping Zhao
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Additional resources for Advances In Biochemical Engineering Biotechnology Biotransformations
G. biotransformations [1a–c, 2], will be very advantageous. In this respect, the hydroxynitrile lyases (Hnl) and their catalytic production of chiral cyanohydrins may have a significant role to play. The Hnls catalyse the asymmetric addition of hydrogen cyanide (HCN) to the carbonyl moiety of an aldehyde or ketone (Scheme 1) to yield a chiral cyanohydrin (1) (where R1 and R2 R1 = Alkyl or Aryl and R2 = H or Alkyl). Reflecting their role in nature, the cyanohydrin is also cleaved by the HNL to yield HCN and the parent carbonyl compound.
Furthermore, their natural substrate is (R)-mandelonitrile. The FAD coenzyme is an important structural feature [18–23] which for Hnl activity is required in its oxidised state [24, 25]; however it is not involved in a redox reaction and may in fact be required for the overall conformational structure of the active enzyme [24–26]. It was suggested by Jorns  that the FAD-containing Hnls may have evolved from a single ancestoral enzyme. In contrast, the non-flavoprotein Hnls are less uniform in their biochemical properties and are isolated from a variety of plant families, such as the seedlings of Linum usitatissimum (flax) [27–29] and Sorghum bicolor (millet) [13, 14, 29–32] and the leaves of Manihot esculenta [33, 34] (manioc), Phlebodium aureum (fern) , Ximenia americana (sandalweed) [36, 37] and Hevea brasiliensis (rubber tree) [38–40].
These may be separated into those with (flavoproteins) Scheme 2. Catabolism of cyanogenic glycosides 34 Table 1. The biochemical properties of seven Hnls Plant Part FAD Co-enzyme Molecular Native Weight (kDa) SDS-page Natural substrate (as glycoside) Ref. V. Johnson · H. Griengl (R)-2-butanone cyanohydrin 27, 28, 29 Plant Part FAD Co-enzyme Molecular Native Weight (kDa) SDS-page Natural substrate (as glycoside) Ref. V. Johnson · H. Griengl and without (non-flavoproteins) the flavin adenine dinucleotide (FAD) coenzyme.