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Review
, 11, 142

Nitrilases in Nitrile Biocatalysis: Recent Progress and Forthcoming Research

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Review

Nitrilases in Nitrile Biocatalysis: Recent Progress and Forthcoming Research

Jin-Song Gong et al. Microb Cell Fact.

Abstract

Over the past decades, nitrilases have drawn considerable attention because of their application in nitrile degradation as prominent biocatalysts. Nitrilases are derived from bacteria, filamentous fungi, yeasts, and plants. In-depth investigations on their natural sources function mechanisms, enzyme structure, screening pathways, and biocatalytic properties have been conducted. Moreover, the immobilization, purification, gene cloning and modifications of nitrilase have been dwelt upon. Some nitrilases are used commercially as biofactories for carboxylic acids production, waste treatment, and surface modification. This critical review summarizes the current status of nitrilase research, and discusses a number of challenges and significant attempts in its further development. Nitrilase is a significant and promising biocatalyst for catalytic applications.

Figures

Figure 1
Figure 1
Number of publications on nitrilase research. Articles (■) were assessed according to Web of Science; patents (□) according to Espacenet search conducted at the end of July 2012.
Figure 2
Figure 2
Putative nitrilase active site [95]. The related residues of Glu54, Lys127 and Cys169 were considered functionally important as a catalytic triad in the nitrilase superfamily.
Figure 3
Figure 3
Proposed mechanism for nitrilase-mediated biocatalysis.
Figure 4
Figure 4
Biosynthesis of nicotinic acid (A), acrylic acid (B), and glycolic acid (C) with nitrilase, respectively.
Figure 5
Figure 5
Biosynthesis of (R)-(−)-mandelic acid from (R,S)-mandelonitrile with nitrilase.

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