Abstract
This article will discuss the importance of specific extremophilic enzymes for applications in industrial biotechnology. It will specifically address those enzymes that have applications in the area of biocatalysis. Such enzymes now play an important role in catalyzing a variety of chemical conversions that were previously carried out by traditional chemistry. The biocatalytic process is carried out under mild conditions and with greater specificity. The enzyme process does not result in the toxic waste that is usually produced in a chemical process that would require careful disposal. In this sense, the biocatalytic process is referred to as carrying out “green chemistry” which is considered to be environmentally friendly. Some of the extremophilic enzymes to be discussed have already been developed for industrial processes such as an l-aminoacylase and a γ-lactamase. The industrial applications of other extremophilic enzymes, including transaminases, carbonic anhydrases, dehalogenases, specific esterases, and epoxide hydrolases, are currently being assessed. Specific examples of these industrially important enzymes that have been studied in the authors group will be presented in this review.
Highlights
A problem with using enzymes for industrial biotransformation reactions is often their inherent stability to the conditions employed
The colonies on the plate that were active showed a brown coloration of the filter paper when the amino acid was produced which had been soaked in ninhydrin stain
The carbonic anhydrase activity requires the presence of a catalytic zinc ion which is coordinated to either histidine or cysteine amino acids depending on the class of the enzyme (Silverman and Lindskog, 1988)
Summary
A problem with using enzymes for industrial biotransformation reactions is often their inherent stability to the conditions employed. The colonies on the plate that were active showed a brown coloration of the filter paper when the amino acid was produced which had been soaked in ninhydrin stain Another non-thermophilic bacterial (+)-γ-lactamase that can carry out this reaction has been identified within the bacterial Delftia species (PDB code 2WKN, Gonsalvez et al, 2001). This enzyme is of a different class, structure, and mechanism from the archaeal enzyme but both can use the non-natural γ-lactam as a substrate. The carbonic anhydrase activity requires the presence of a catalytic zinc ion which is coordinated to either histidine or cysteine amino acids depending on the class of the enzyme (Silverman and Lindskog, 1988)
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