Chapter 4
State of the Art and Outlook
The biotransformations described in this book demonstrate that this area is in
an active state of development and that enzymes have attained an important
position in contemporary organic synthesis both on the academic and the industrial
level [1–10]. The increased interest of synthetic chemists in the biotransformation
of nonnatural compounds has spurred the commercial availability of enzymes in
various forms and grades of purity [11, 12]. To date, about $8 % of all papers
published in the area of synthetic organic chemistry contain elements of biotransformations [13] and >300 industrial-scale processes are documented worldwide
[14–24]. As shown in Fig. 4.1, the frequency of use of a particular biocatalyst is not
evenly distributed among the various types of enzymes and it is obvious that the
more ‘simple’ hydrolytic reactions are dominant.
1 In this book, attention has been
focused on those methods which are most useful for and accessible to synthetic
chemists and the rating of methods according to their general applicability and
reliability is intended!
In the following paragraphs a brief summary on the state of the art of biotransformations is given (Table 4.1) with an outlook on future developments.
Hydrolytic enzymes such as proteases, esterases and lipases are ready-to-use
catalysts for the preparation of optically active carboxylic acids, amino acids,
alcohols, and amines. This reliable technology is applicable to a broad range of
synthetic problems and is widely used in industry. The broad knowledge on biotransformations from these areas has evolved a large number of commercially
available proteases and lipases in conjunction with their substrate tolerance and
techniques for the improvement of their selectivities and predictive models for the
stereochemical outcome of a given reaction. A search for novel esterases to enrich
the limited number of available enzymes and for lipases showing ‘anti-Kazlauskas’
stereo-specificities would be a worthwhile endeavor.
1 Data from database Kroutil/Faber, ~18,000 entries, 2016.
© Springer International Publishing AG 2018
K. Faber, Biotransformations in Organic Chemistry,
DOI 10.1007/978-3-319-61590-5_4
407
State of the Art and Outlook
The biotransformations described in this book demonstrate that this area is in
an active state of development and that enzymes have attained an important
position in contemporary organic synthesis both on the academic and the industrial
level [1–10]. The increased interest of synthetic chemists in the biotransformation
of nonnatural compounds has spurred the commercial availability of enzymes in
various forms and grades of purity [11, 12]. To date, about $8 % of all papers
published in the area of synthetic organic chemistry contain elements of biotransformations [13] and >300 industrial-scale processes are documented worldwide
[14–24]. As shown in Fig. 4.1, the frequency of use of a particular biocatalyst is not
evenly distributed among the various types of enzymes and it is obvious that the
more ‘simple’ hydrolytic reactions are dominant.
1 In this book, attention has been
focused on those methods which are most useful for and accessible to synthetic
chemists and the rating of methods according to their general applicability and
reliability is intended!
In the following paragraphs a brief summary on the state of the art of biotransformations is given (Table 4.1) with an outlook on future developments.
Hydrolytic enzymes such as proteases, esterases and lipases are ready-to-use
catalysts for the preparation of optically active carboxylic acids, amino acids,
alcohols, and amines. This reliable technology is applicable to a broad range of
synthetic problems and is widely used in industry. The broad knowledge on biotransformations from these areas has evolved a large number of commercially
available proteases and lipases in conjunction with their substrate tolerance and
techniques for the improvement of their selectivities and predictive models for the
stereochemical outcome of a given reaction. A search for novel esterases to enrich
the limited number of available enzymes and for lipases showing ‘anti-Kazlauskas’
stereo-specificities would be a worthwhile endeavor.
1 Data from database Kroutil/Faber, ~18,000 entries, 2016.
© Springer International Publishing AG 2018
K. Faber, Biotransformations in Organic Chemistry,
DOI 10.1007/978-3-319-61590-5_4
407