NDLI: Biochemistry and biotechnology of mesophilic and thermophilic nitrile metabolizing enzymes

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Biochemistry and biotechnology of mesophilic and thermophilic nitrile metabolizing enzymes

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Extremophiles : Volume 2, Issue 2, May 1998

Extremophiles : Volume 2, Issue 1, February 1998

Extremophiles : Volume 1

Biochemistry and biotechnology of mesophilic and thermophilic nitrile metabolizing enzymes

Content Provider	Springer Nature Link
Author	Cowan, D. Cramp, Rebecca Pereira, R. Graham, D. Almatawah, Qadreyah
Copyright Year	1998
Abstract	Mesophilic nitrile-degrading enzymes are widely dispersed in the Bacteria and lower orders of the eukaryotic kingdom. Two distinct enzyme systems, a nitrilase catalyzing the direct conversion of nitriles to carboxylic acids and separate but cotranscribed nitrile hydratase and amidase activities, are now well known. Nitrile hydratases are metalloenzymes, incorporating FeIII or CoII ions in thiolate ligand networks where they function as Lewis acids. In comparison, nitrilases are thiol-enzymes and the two enzyme groups have little or no apparent sequence or structural homology. The hydratases typically exist as αβ dimers or tetramers in which the α- and β-subunits are similar in size but otherwise unrelated. Nitrilases however, are usually found as homomultimers with as many as 16 subunits. Until recently, the two nitrile-degrading enzyme classes were clearly separated by functional differences, the nitrile hydratases being aliphatic substrate specific and lacking stereoselectivity, whereas the nitrilases are enantioselective and aromatic substrate specific. The recent discovery of novel enzymes in both classes (including thermophilic representatives) has blurred these functional distinctions. Purified mesophilic nitrile-degrading enzymes are typically thermolabile in buffered solution, rarely withstanding exposure to temperatures above 50°C without rapid inactivation. However, operational thermostability is often increased by addition of aliphatic acids or by use of immobilized whole cells. Low molecular stability has frequently been cited as a reason for the limited industrial application of "nitrilases"; such statements notwithstanding, these enzymes have been successfully applied for more than a decade to the kiloton production of acrylamide and more recently to the smaller-scale production of nicotinic acid, R-(−)-mandelic acid and S-(+)-ibuprofen. There is also a rapidly growing catalog of other potentially useful conversions of complex nitriles in which the regioselectivity of the enzyme coupled with the ability to achieve high conversion efficiencies without detriment to other sensitive functionalities is a distinct process advantage.
Starting Page	207
Ending Page	216
Page Count	10
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	2
Issue Number	3
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-08-20
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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