The catalytic properties of some selected enzymes have long been exploited to carry out efficient and cost-effective-bioconversions in a multitude of research and industrial sectors, such as food, health, cosmetics, agriculture, chemistry, energy, and others. Nonetheless, for several applications, naturally occurring enzymes are not considered to be viable options owing to their limited stability in the required working conditions. Over the years, the quest for novel enzymes with actual potential for biotechnological applications has involved various complementary approaches such as mining enzyme variants from organisms living in extreme conditions (extremophiles), mimicking evolution in the laboratory to develop more stable enzyme variants, and more recently, using rational, computer-assisted enzyme engineering strategies. In this review, we provide an overview of the most relevant enzymes that are used for industrial applications and we discuss the strategies that are adopted to enhance enzyme stability and/or activity, along with some of the most relevant achievements. In all living species, many different enzymes catalyze fundamental chemical reactions with high substrate specificity and rate enhancements. Besides specificity, enzymes also possess many other favorable properties, such as, for instance, cost-effectiveness, good stability under mild pH and temperature conditions, generally low toxicity levels, and ease of termination of activity. As efficient natural biocatalysts, enzymes provide great opportunities to carry out important chemical reactions in several research and industrial settings, ranging from food to pharmaceutical, cosmetic, agricultural, and other crucial economic sectors. (C) 2018 Author(s).

Rigoldi, F., Donini, S., Redaelli, A., Parisini, E., Gautieri, A. (2018). Review: Engineering of thermostable enzymes for industrial applications. APL BIOENGINEERING, 2(1), 1-17 [10.1063/1.4997367].

Review: Engineering of thermostable enzymes for industrial applications

Parisini, Emilio
;
2018

Abstract

The catalytic properties of some selected enzymes have long been exploited to carry out efficient and cost-effective-bioconversions in a multitude of research and industrial sectors, such as food, health, cosmetics, agriculture, chemistry, energy, and others. Nonetheless, for several applications, naturally occurring enzymes are not considered to be viable options owing to their limited stability in the required working conditions. Over the years, the quest for novel enzymes with actual potential for biotechnological applications has involved various complementary approaches such as mining enzyme variants from organisms living in extreme conditions (extremophiles), mimicking evolution in the laboratory to develop more stable enzyme variants, and more recently, using rational, computer-assisted enzyme engineering strategies. In this review, we provide an overview of the most relevant enzymes that are used for industrial applications and we discuss the strategies that are adopted to enhance enzyme stability and/or activity, along with some of the most relevant achievements. In all living species, many different enzymes catalyze fundamental chemical reactions with high substrate specificity and rate enhancements. Besides specificity, enzymes also possess many other favorable properties, such as, for instance, cost-effectiveness, good stability under mild pH and temperature conditions, generally low toxicity levels, and ease of termination of activity. As efficient natural biocatalysts, enzymes provide great opportunities to carry out important chemical reactions in several research and industrial settings, ranging from food to pharmaceutical, cosmetic, agricultural, and other crucial economic sectors. (C) 2018 Author(s).
2018
Rigoldi, F., Donini, S., Redaelli, A., Parisini, E., Gautieri, A. (2018). Review: Engineering of thermostable enzymes for industrial applications. APL BIOENGINEERING, 2(1), 1-17 [10.1063/1.4997367].
Rigoldi, Federica; Donini, Stefano; Redaelli, Alberto; Parisini, Emilio; Gautieri, Alfonso
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/915355
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