Frontier in Biocatalysis and Biotransformations

Topic Information

Dear Colleagues,

In recent years, many new biocatalysts have been described and studied mostly from a biocatalytic perspective. Since more and more (meta)genome data become available, even more of those studies will appear and add to our knowledge on novel reactions and enzymes. However, the transfer to application needs more attention and, thus, scale-up. Enzyme production and optimization in combination with product isolation also need more attention. Thus, this Topic aims to focus on this chain, including the identification of novel enzymes from bioprospecting activities, producing enzymes and increasing yields from various host organisms, engineering biocatalysts by means of site-directed mutagenesis or directed evolution, putting enzymes together—even with chemical synthesis—yielding novel chemoenzymatic cascades, product isolation after processing or in situ, and even combinatorial approaches towards new products. All this needs research in the field of biocatalysis and biotransformation to bring us to new frontiers.

Asst. Prof. Dr. Dirk Tischler
Topic Editor

Keywords

Participating Journals

Journal Name	Impact Factor	CiteScore	Launched Year	First Decision (median)	APC
Applied Sciences applsci	2.5	5.3	2011	17.8 Days	CHF 2400
BioTech biotech	2.7	3.7	2012	18.2 Days	CHF 1600
Catalysts catalysts	3.8	6.8	2011	12.9 Days	CHF 2200
International Journal of Environmental Research and Public Health ijerph	-	7.3	2004	24.3 Days	CHF 2500
Processes processes	2.8	5.1	2013	14.4 Days	CHF 2400

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Published Papers (4 papers)

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11 pages, 1405 KiB  

Open AccessArticle

Exploring the Strategy of Fusing Sucrose Synthase to Glycosyltransferase UGT76G1 in Enzymatic Biotransformation

by Yehui Tao, Ping Sun, Ruxin Cai, Yan Li and Honghua Jia

Appl. Sci. 2022, 12(8), 3911; https://doi.org/10.3390/app12083911 - 13 Apr 2022

Cited by 2 | Viewed by 2475

Abstract

Uridine diphosphate glycosyltransferases (UGTs) as fine catalysts of glycosylation are increasingly used in the synthesis of natural products. Sucrose synthase (SuSy) is recognized as a powerful tool for in situ regenerating sugar donors for the UGT-catalyzed reaction. It is crucial to select the [...] Read more.

Uridine diphosphate glycosyltransferases (UGTs) as fine catalysts of glycosylation are increasingly used in the synthesis of natural products. Sucrose synthase (SuSy) is recognized as a powerful tool for in situ regenerating sugar donors for the UGT-catalyzed reaction. It is crucial to select the appropriate SuSy for cooperation with UGT in a suitable way. In the present study, eukaryotic SuSy from Arabidopsisthaliana (AtSUS1) helped stevia glycosyltransferase UGT76G1 achieve the complete conversion of stevioside (30 g/L) into rebaudioside A (RebA). Position of the individual transcription units containing the genes encoding AtSUS1 and UGT76G1 in the expression plasmid has an effect, but less than that of the fusion order of these genes on RebA yield. Fusion of the C-terminal of AtSUS1 and the N-terminal of UGT76G1 with rigid linkers are conducive to maintaining enzyme activities. When the same fusion strategy was applied to a L637M-T640V double mutant of prokaryotic SuSy from Acidithiobacillus caldus (AcSuSym), 18.8 ± 0.6 g/L RebA (a yield of 78.2%) was accumulated in the reaction mixture catalyzed by the fusion protein Acm-R3-76G1 (the C-terminal of AcSuSym and the N-terminal of UGT76G1 were linked with (EAAAK)3). This work would hopefully reveal the potential of UGT-SuSy fusion in improving the cascade enzymatic glycosylation. Full article

(This article belongs to the Topic Frontier in Biocatalysis and Biotransformations)
(This article belongs to the Section Applied Biosciences and Bioengineering)

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19 pages, 2570 KiB  

Open AccessArticle

Characterization of Two Hydrogen Peroxide Resistant Peroxidases from Rhodococcus opacus 1CP

by Anna Christina R. Ngo, Catleen Conrad, Álvaro Gómez Baraibar, Anke Matura, Karl-Heinz van Pée and Dirk Tischler

Appl. Sci. 2021, 11(17), 7941; https://doi.org/10.3390/app11177941 - 27 Aug 2021

Cited by 5 | Viewed by 2520

Abstract

The dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such as azo dyes or anthraquinones make them [...] Read more.

The dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such as azo dyes or anthraquinones make them excellent candidates for applications in bioremediation and organic synthesis. In this work, two novel DyP peroxidases from the organism Rhodococcus opacus 1CP (DypA and DypB) were cloned and expressed in Escherichia coli. The enzymes were purified and biochemically characterized. The activities of the two DyPs via 2,2′-azino-bis [3-ethylbenzthiazoline-6-sulphonic acid] (ABTS) assay and against Reactive Blue 5 were assessed and optimized. Results showed varying trends for DypA and DypB. Remarkably, these enzymes presented a particularly high tolerance towards H₂O₂, retaining its activities at about 10 mM H₂O₂ for DypA and about 4.9 mM H₂O₂ for DypB. Full article

(This article belongs to the Topic Frontier in Biocatalysis and Biotransformations)
(This article belongs to the Section Applied Biosciences and Bioengineering)

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11 pages, 998 KiB  

Open AccessCommunication

Enzymatically Synthesized Ginsenoside Exhibits Antiproliferative Activity in Various Cancer Cell Lines

by Sumangala Darsandhari, Biplav Shrestha, Ramesh Prasad Pandey, Sanghun Lee, Hye Jin Jung, Yeon Ju Kim and Jae Kyung Sohng

Appl. Sci. 2019, 9(5), 893; https://doi.org/10.3390/app9050893 - 2 Mar 2019

Cited by 4 | Viewed by 3957

Abstract

A glycoside derivative of compound K (CK) was synthesized by using a glycosyltransferase, and its biological activity was tested against various cancer-cell lines. A regiospecific, β-1,4-galactosyltransferase (LgtB) converted 100% of 0.5 mmol CK into a galactosylated product in 3 h. The structure of [...] Read more.

A glycoside derivative of compound K (CK) was synthesized by using a glycosyltransferase, and its biological activity was tested against various cancer-cell lines. A regiospecific, β-1,4-galactosyltransferase (LgtB) converted 100% of 0.5 mmol CK into a galactosylated product in 3 h. The structure of the synthesized derivative was revealed with high performance liquid chromatography, mass spectroscopy, as well as nuclear magnetic resonance analyses, and it was recognized as 20-O-β-D-lactopyranosyl-20(S)-protopanaxadiol (CKGal). Out of the four cancer-cell lines tested (gastric carcinoma (AGS), skin melanoma (B16F10), cervical carcinoma (HeLa), and brain carcinoma (U87MG)), CKGal showed the best cytotoxic ability against B16F10 and AGS when compared to other ginsenosides like compound K (20-O-β-D-glucopyranosyl-20(S)-protopanaxadiol), Rh2 (3-O-β-D-glucopyranosyl-20(S)-protopanaxadiol), and F12 (3-O-β-D-glucopyranosyl-12-O-β-D-glucopyranosyl-20(S)-protopanaxadiol). Thus, the synthesized derivative (CKGal) is a pharmacologically active ginsenoside. Full article

(This article belongs to the Topic Frontier in Biocatalysis and Biotransformations)
(This article belongs to the Section Applied Biosciences and Bioengineering)

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11 pages, 1104 KiB  

Open AccessArticle

A Synthetic Approach for Biosynthesis of Miquelianin and Scutellarin A in Escherichia coli

by Ramesh Prasad Pandey, Ha Young Jung, Prakash Parajuli, Thi Huyen Trang Nguyen, Puspalata Bashyal and Jae Kyung Sohng

Appl. Sci. 2019, 9(2), 215; https://doi.org/10.3390/app9020215 - 9 Jan 2019

Cited by 5 | Viewed by 5277

Abstract

Grapevine (Vitis vinifera) glycucuronosyltransferase (VvGT5) specifically catalyzes flavonol-3-O-glucuronosylation and the blue flowers of Veronica persica (Lamiales, Scrophulariaceae) uridine diphosphate (UDP)-dependent glycosyltransferase (UGT88D8) as flavonoid 7-O-specific glucuronosyltransferases, were chosen, codon optimized, and employed to synthesize the high valued [...] Read more.

Grapevine (Vitis vinifera) glycucuronosyltransferase (VvGT5) specifically catalyzes flavonol-3-O-glucuronosylation and the blue flowers of Veronica persica (Lamiales, Scrophulariaceae) uridine diphosphate (UDP)-dependent glycosyltransferase (UGT88D8) as flavonoid 7-O-specific glucuronosyltransferases, were chosen, codon optimized, and employed to synthesize the high valued flavonoids glucuronoids, miquelianin and scutellarin A in Escherichia coli. A single vector system was constructed to overexpress entire UDP-glucuronic acid biosynthesis pathway genes, along with a glucokinase gene in Escherichia coli BL21 (DE3). The newly generated E. coli BL21 (DE3) piBR181-glk.pgm2.galU.ugd.UGT88D8 strain produced 12 mg/L (28 µmol/L) of scutellarin A from apigenin, representing only 14% of maximum conversion percentage. Similarly, the strain E. coli BL21 (DE3) piBR181-glk.pgm2.galU.ugd.VvGT5 produced 30 mg/L (62 µmol/L) of miquelianin, representing a 31% conversion of quercetin. This production profile is a good starting point for further host engineering, and for production of respective compounds. Full article

(This article belongs to the Topic Frontier in Biocatalysis and Biotransformations)
(This article belongs to the Section Applied Biosciences and Bioengineering)

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