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Enzyme Biocatalysts: Design and Application

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Editorial02 February 2022
Editorial: Enzyme Biocatalysts: Design and Application

protein engineering approach, catalysis with enzymes, i.e., biocatalysis, has emerged as the most powerful technology for widespread industrial applications by minimizing waste, reducing energy necessities, and increasing catalytic reactions (Sheldon et al., 2020;Wu et al., 2021). Enzymes are highly efficient, biocompatible, and biodegradable catalysts and are likely to be produced from bio-renewable resources. In contrast to chemical catalysts, enzymatic reactions are carried out at nearly ambient pressures and temperatures at physiological pH, leading to high reaction rates and selectivity.Moreover, protection or activation of functional groups is not required, and enzymemediated biocatalytic processes are atom and step economic, resulting in minimal waste and energy consumption than traditional counterparts. To sum up, biocatalytic processes are more economical, sustainable and possess a lower environmental footprint compared to conventional traditional processes for manufacturing commodity chemicals (Sheldon et al., 2021).Therefore, enzymes have gained booming importance for producing valuable chemicals, pharmaceuticals, agrochemicals, fuels, and other commodity bio-products in industrial processes. Nevertheless, the fragile nature of native enzymes prevents their utilization under challenging environments, where the industrial bioprocesses generally execute, causing low activity and inadequate stability. A number of approaches, including enzyme immobilization, chemical modifications, Integrated chemo-and biocatalysis, and designing (micro)environments for biocatalysts, have become the rapidly expanding areas of research to develop industrial biocatalysts with aggrandized stabilities, exquisite selectivities, and special activities with non-natural substrates in the unfavourable milieu of high temperatures and elevated substrate concentrations (Ren et al., 2019). In the last two decades, biocatalysis has witnessed immense progress and phenomenal growth for transforming into a mature technology with a vast industrial perspective. This development was mainly attributed to the advances in genomics, biochemistry, bioinformatics, synthetic biology, protein engineering, and other computational tools (Bilal et al., 2019).In total, 7 articles were published in this Research Topic summarizing various aspects of enzymes like identification, characterization, improving catalytic attributes and applications in multiple sectors. These were not explicitly focused on a specific domain and relatively more comprehensively, connecting new enzymes' exploration with their biocatalytic applications.

All listed author(s) are thankful to their representative universities/institutes for providing the related support to compile this work.

The listed author(s) declare no conflict of interest in any capacity, including competing or financial.

All listed author(s) have made a substantial, direct and intellectual contribution to the work, and approved it for publication.

2,983 views

1 citations

MINI REVIEW
19 August 2021
Sulfoxide Reductases and Applications in Biocatalytic Preparation of Chiral Sulfoxides: A Mini-Review
Tao Peng, 2 more and Jiawei Yang
Sulfoxide Reductases and Applications in Biocatalytic Preparation of Chiral Sulfoxides: A Mini-Review
Chiral sulfoxides are valuable organosulfur compounds that being widely used in medicinal and organic synthesis chemistry. Biocatalytic approaches for the preparation of chiral sulfoxides were developed in past few years, mainly through asymmetric oxidation of prochiral sulfides. Recently, application of sulfoxide reductase to prepare chiral sulfoxides through kinetic resolution has emerged as a new method, exhibiting excellent catalytic properties. This paper reviews the finding, chemistry and biological function of these sulfoxide reductases and highlights their applications in chiral sulfoxide preparation.

7,481 views

26 citations

ORIGINAL RESEARCH
16 July 2021
Construction of T7-Like Expression System in Pseudomonas putida KT2440 to Enhance the Heterologous Expression Level
Tianxin Liang, 4 more and Jianping Wu

7,752 views

15 citations

MINI REVIEW
31 May 2021
Application Fields, Positions, and Bioinformatic Mining of Non-active Sites: A Mini-Review
Xiaoxiao Wang, 4 more and Liming Zhao

2,927 views

5 citations

Improving the Thermostability and Activity of Transaminase From Aspergillus terreus by Charge-Charge Interaction
ORIGINAL RESEARCH
14 April 2021
Improving the Thermostability and Activity of Transaminase From Aspergillus terreus by Charge-Charge Interaction
Jia-Ren Cao, 8 more and Le-He Mei

10,895 views

41 citations

Exploring the Potential of Cytochrome P450 CYP109B1 Catalyzed Regio—and Stereoselective Steroid Hydroxylation
ORIGINAL RESEARCH
18 February 2021
Exploring the Potential of Cytochrome P450 CYP109B1 Catalyzed Regio—and Stereoselective Steroid Hydroxylation
Xiaodong Zhang, 5 more and Aitao Li

8,627 views

31 citations

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta
ORIGINAL RESEARCH
10 December 2020
Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta
Yang Wang, 6 more and Wenjing Sun
D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEases that works at acidic conditions are highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was identified and characterized from human intestinal gut bacterium, Christensenella minuta. The catalytic activity of dte on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The addition of Ni2+ not only enhanced the enzyme activity, but also resulted in improving the enzyme half-life at 50℃ from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50 ℃ with a Kcat/Km value of 45 mM-1min-1. The enzymatic conversion of D-fructose into D-allulose using this enzyme produced 156 g/L D-allulose from 500 g/L D-fructose, which corresponded to 30 % conversion efficiency. With these interesting catalytic properties, the enzyme could be a promising candidate for industrial biocatalytic applications.

8,108 views

39 citations