Bioprospecting of Novel Extremozymes From Prokaryotes—The Advent of Culture-Independent Methods

In a global context where the development of more environmentally conscious technologies is an urgent need, the demand for enzymes for industrial processes is on the rise. Compared to conventional chemical catalysts, the implementation of biocatalysis presents important benefits including higher selectivity, increased sustainability, reduction in operating costs and low toxicity, which translate into cleaner production processes, lower environmental impact as well as increasing the safety of the operating staff. Most of the currently available commercial enzymes are of mesophilic origin, displaying optimal activity in narrow ranges of conditions, which limits their actual application under industrial settings. For this reason, enzymes from extremophilic microorganisms stand out for their specific characteristics, showing higher stability, activity and robustness than their mesophilic counterparts. Their unique structural adaptations allow them to resist denaturation at high temperatures and salinity, remain active at low temperatures, function at extremely acidic or alkaline pHs and high pressure, and participate in reactions in organic solvents and unconventional media. Because of the increased interest to replace chemical catalysts, the global enzymes market is continuously growing, with hydrolases being the most prominent type of enzymes, holding approximately two-third share, followed by oxidoreductases. The latter enzymes catalyze electron transfer reactions and are one of the most abundant classes of enzymes within cells. They hold a significant industrial potential, especially those from extremophiles, as their applications are multifold. In this article we aim to review the properties and potential applications of five different types of extremophilic oxidoreductases: laccases, hydrogenases, glutamate dehydrogenases (GDHs), catalases and superoxide dismutases (SODs). This selection is based on the extensive experience of our research group working with these particular enzymes, from the discovery up to the development of commercial products available for the research market.

Section: Discovery Development and Production Of Novel Extremophilic Oxidoreductasesmentioning

confidence: 99%

Section: Discovery Development and Production Of Novel Extremophilic Oxidoreductasesmentioning

confidence: 99%

Extremophilic Oxidoreductases for the Industry: Five Successful Examples With Promising Projections

Espina

Atalah

Blamey

2021

“…From an industrial point of view, the ideal biocatalyst must be stable and active under processing conditions, have suitable substrate specificity, regio-and enantioselectivity, be efficient and produce the required product within a suitable time with little to no byproducts and minimal product-inhibition ( Lorenz and Eck 2005 ). Most enzymes available originate from mesophilic organisms, and their narrow range of stability limits their use in many applications ( Sysoev et al, 2021 ). Enzymes derived from extremophiles, called extremozymes, overcome these limitations.…”

Section: Introductionmentioning

confidence: 99%

Industrial Biotechnology Based on Enzymes From Extreme Environments

Mesbah

2022

Biocatalysis is crucial for a green, sustainable, biobased economy, and this has driven major advances in biotechnology and biocatalysis over the past 2 decades. There are numerous benefits to biocatalysis, including increased selectivity and specificity, reduced operating costs and lower toxicity, all of which result in lower environmental impact of industrial processes. Most enzymes available commercially are active and stable under a narrow range of conditions, and quickly lose activity at extremes of ion concentration, temperature, pH, pressure, and solvent concentrations. Extremophilic microorganisms thrive under extreme conditions and produce robust enzymes with higher activity and stability under unconventional circumstances. The number of extremophilic enzymes, or extremozymes, currently available are insufficient to meet growing industrial demand. This is in part due to difficulty in cultivation of extremophiles in a laboratory setting. This review will present an overview of extremozymes and their biotechnological applications. Culture-independent and genomic-based methods for study of extremozymes will be presented.

“…To date, there are two main approaches to discover novel extremozymes from environmental samples. On one hand, due to the inherent difficulty and specific requirements of in vitro culturing of extremophilic microorganisms, especially archaea, there is a culture independent approach, which is based on metagenomic sequencing followed by data mining to search for specific genes that potentially codify for an enzyme of interest ( Sysoev et al, 2021 ). However, one disadvantage of this strategy is that to date, there is a lack of reliable functional annotation of extremophile genomic data, caused by the low amount of experimentally described genes.…”

Section: Introductionmentioning

confidence: 99%

From the Discovery of Extremozymes to an Enzymatic Product: Roadmap Based on Their Applications

Espina

Muñoz-Ibacache

Cáceres-Moreno

et al. 2022

With the advent of the industrial revolution, the use of toxic compounds has grown exponentially, leading to a considerable pollution of the environment. Consequently, the development of more environmentally conscious technologies is an urgent need. Industrial biocatalysis appears as one potential solution, where a higher demand for more robust enzymes aims to replace toxic chemical catalysts. To date, most of the commercially available enzymes are of mesophilic origin, displaying optimal activity in narrow ranges of temperature and pH (i.e., between 20°C and 45°C, neutral pH), limiting their actual application under industrial reaction settings, where they usually underperform, requiring larger quantities to compensate loss of activity. In order to obtain novel biocatalysts better suited for industrial conditions, an efficient solution is to take advantage of nature by searching and discovering enzymes from extremophiles. These microorganisms and their macromolecules have already adapted to thrive in environments that present extreme physicochemical conditions. Hence, extremophilic enzymes stand out for showing higher activity, stability, and robustness than their mesophilic counterparts, being able to carry out reactions at nonstandard conditions. In this brief research report we describe three examples to illustrate a stepwise strategy for the development and production of commercial extremozymes, including a catalase from an Antarctic psychrotolerant microorganism, a laccase from a thermoalkaliphilic bacterium isolated from a hot spring and an amine-transaminase from a thermophilic bacterium isolated from a geothermal site in Antarctica. We will also explore some of their interesting biotechnological applications and comparisons with commercial enzymes.