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Degradation of biological macromolecules supports uncultured microbial populations in Guaymas Basin hydrothermal sediments.

The ISME journal

Pérez Castro S, Borton MA, Regan K, Hrabe de Angelis I, Wrighton KC, Teske AP, Strous M, Ruff SE.
PMID: 34112968
ISME J. 2021 Dec;15(12):3480-3497. doi: 10.1038/s41396-021-01026-5. Epub 2021 Jun 10.

Hydrothermal sediments contain large numbers of uncultured heterotrophic microbial lineages. Here, we amended Guaymas Basin sediments with proteins, polysaccharides, nucleic acids or lipids under different redox conditions and cultivated heterotrophic thermophiles with the genomic potential for macromolecule degradation. We...

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Pérez Castro S, Borton MA, Regan K, et al. Degradation of biological macromolecules supports uncultured microbial populations in Guaymas Basin hydrothermal sediments. ISME J. 2021;15(12):3480-3497doi: 10.1038/s41396-021-01026-5.
Pérez Castro, S., Borton, M. A., Regan, K., Hrabe de Angelis, I., Wrighton, K. C., Teske, A. P., Strous, M., & Ruff, S. E. (2021). Degradation of biological macromolecules supports uncultured microbial populations in Guaymas Basin hydrothermal sediments. The ISME journal, 15(12), 3480-3497. https://doi.org/10.1038/s41396-021-01026-5
Pérez Castro, Sherlynette, et al. "Degradation of biological macromolecules supports uncultured microbial populations in Guaymas Basin hydrothermal sediments." The ISME journal vol. 15,12 (2021): 3480-3497. doi: https://doi.org/10.1038/s41396-021-01026-5
Pérez Castro S, Borton MA, Regan K, Hrabe de Angelis I, Wrighton KC, Teske AP, Strous M, Ruff SE. Degradation of biological macromolecules supports uncultured microbial populations in Guaymas Basin hydrothermal sediments. ISME J. 2021 Dec;15(12):3480-3497. doi: 10.1038/s41396-021-01026-5. Epub 2021 Jun 10. PMID: 34112968; PMCID: PMC8630151.
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Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency.

Biotechnology for biofuels

Rubio MV, Terrasan CRF, Contesini FJ, Zubieta MP, Gerhardt JA, Oliveira LC, de Souza Schmidt Gonçalves AE, Almeida F, Smith BJ, de Souza GHMF, Dias AHS, Skaf M, Damasio A.
PMID: 31754374
Biotechnol Biofuels. 2019 Nov 14;12:269. doi: 10.1186/s13068-019-1609-2. eCollection 2019.

BACKGROUND: β-Xylosidases are glycoside hydrolases (GHs) that cleave xylooligosaccharides and/or xylobiose into shorter oligosaccharides and xylose. RESULTS: In this study, BxlB-a highly secreted GH3 β-xylosidase from CONCLUSIONS: This study demonstrates the influence of N-glycosylation on

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Rubio MV, Terrasan CRF, Contesini FJ, et al. Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency. Biotechnol Biofuels. 2019;12:269doi: 10.1186/s13068-019-1609-2.
Rubio, M. V., Terrasan, C. R. F., Contesini, F. J., Zubieta, M. P., Gerhardt, J. A., Oliveira, L. C., de Souza Schmidt Gonçalves, A. E., Almeida, F., Smith, B. J., de Souza, G. H. M. F., Dias, A. H. S., Skaf, M., & Damasio, A. (2019). Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency. Biotechnology for biofuels, 12269. https://doi.org/10.1186/s13068-019-1609-2
Rubio, Marcelo Ventura, et al. "Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency." Biotechnology for biofuels vol. 12 (2019): 269. doi: https://doi.org/10.1186/s13068-019-1609-2
Rubio MV, Terrasan CRF, Contesini FJ, Zubieta MP, Gerhardt JA, Oliveira LC, de Souza Schmidt Gonçalves AE, Almeida F, Smith BJ, de Souza GHMF, Dias AHS, Skaf M, Damasio A. Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency. Biotechnol Biofuels. 2019 Nov 14;12:269. doi: 10.1186/s13068-019-1609-2. eCollection 2019. PMID: 31754374; PMCID: PMC6854716.
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Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.

The Journal of biological chemistry

Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T.
PMID: 34728215
J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30.

Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on α-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to...

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Nakamura S, Nihira T, Kurata R, et al. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021;297(6):101366doi: 10.1016/j.jbc.2021.101366.
Nakamura, S., Nihira, T., Kurata, R., Nakai, H., Funane, K., Park, E. Y., & Miyazaki, T. (2021). Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. The Journal of biological chemistry, 297(6), 101366. https://doi.org/10.1016/j.jbc.2021.101366
Nakamura, Shuntaro, et al. "Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases." The Journal of biological chemistry vol. 297,6 (2021): 101366. doi: https://doi.org/10.1016/j.jbc.2021.101366
Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30. PMID: 34728215; PMCID: PMC8626586.
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Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.

The Journal of biological chemistry

Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T.
PMID: 34728215
J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30.

Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on α-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to...

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Nakamura S, Nihira T, Kurata R, et al. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021;297(6):101366doi: 10.1016/j.jbc.2021.101366.
Nakamura, S., Nihira, T., Kurata, R., Nakai, H., Funane, K., Park, E. Y., & Miyazaki, T. (2021). Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. The Journal of biological chemistry, 297(6), 101366. https://doi.org/10.1016/j.jbc.2021.101366
Nakamura, Shuntaro, et al. "Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases." The Journal of biological chemistry vol. 297,6 (2021): 101366. doi: https://doi.org/10.1016/j.jbc.2021.101366
Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30. PMID: 34728215; PMCID: PMC8626586.
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Effect of solid loading on the behaviour of pectin-degrading enzymes.

Biotechnology for biofuels

Li F, Foucat L, Bonnin E.
PMID: 33910612
Biotechnol Biofuels. 2021 Apr 28;14(1):107. doi: 10.1186/s13068-021-01957-3.

BACKGROUND: Pectin plays a role in the recalcitrance of plant biomass by affecting the accessibility of other cell wall components to enzymatic degradation. Elimination of pectin consequently has a positive impact on the saccharification of pectin-rich biomass. This work...

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Li F, Foucat L, Bonnin E. Effect of solid loading on the behaviour of pectin-degrading enzymes. Biotechnol Biofuels. 2021;14(1):107doi: 10.1186/s13068-021-01957-3.
Li, F., Foucat, L., & Bonnin, E. (2021). Effect of solid loading on the behaviour of pectin-degrading enzymes. Biotechnology for biofuels, 14(1), 107. https://doi.org/10.1186/s13068-021-01957-3
Li, Fan, et al. "Effect of solid loading on the behaviour of pectin-degrading enzymes." Biotechnology for biofuels vol. 14,1 (2021): 107. doi: https://doi.org/10.1186/s13068-021-01957-3
Li F, Foucat L, Bonnin E. Effect of solid loading on the behaviour of pectin-degrading enzymes. Biotechnol Biofuels. 2021 Apr 28;14(1):107. doi: 10.1186/s13068-021-01957-3. PMID: 33910612; PMCID: PMC8082855.
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Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.

Frontiers in bioengineering and biotechnology

Sidar A, Albuquerque ED, Voshol GP, Ram AFJ, Vijgenboom E, Punt PJ.
PMID: 32850729
Front Bioeng Biotechnol. 2020 Jul 31;8:871. doi: 10.3389/fbioe.2020.00871. eCollection 2020.

Enzymatic degradation of abundant renewable polysaccharides such as cellulose and starch is a field that has the attention of both the industrial and scientific community. Most of the polysaccharide degrading enzymes are classified into several glycoside hydrolase families. They...

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Sidar A, Albuquerque ED, Voshol GP, et al. Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms. Front Bioeng Biotechnol. 2020;8:871doi: 10.3389/fbioe.2020.00871.
Sidar, A., Albuquerque, E. D., Voshol, G. P., Ram, A. F. J., Vijgenboom, E., & Punt, P. J. (2020). Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms. Frontiers in bioengineering and biotechnology, 8871. https://doi.org/10.3389/fbioe.2020.00871
Sidar, Andika, et al. "Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms." Frontiers in bioengineering and biotechnology vol. 8 (2020): 871. doi: https://doi.org/10.3389/fbioe.2020.00871
Sidar A, Albuquerque ED, Voshol GP, Ram AFJ, Vijgenboom E, Punt PJ. Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms. Front Bioeng Biotechnol. 2020 Jul 31;8:871. doi: 10.3389/fbioe.2020.00871. eCollection 2020. PMID: 32850729; PMCID: PMC7410926.
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Construction of a novel filamentous fungal protein expression system based on redesigning of regulatory elements.

Applied microbiology and biotechnology

Zhang Z, Xiang B, Zhao S, Yang L, Chen Y, Hu Y, Hu S.
PMID: 35019997
Appl Microbiol Biotechnol. 2022 Jan;106(2):647-661. doi: 10.1007/s00253-022-11761-0. Epub 2022 Jan 12.

Filamentous fungi are extensively used as an important expression host for the production of a variety of essential industrial proteins. They have significant promise as an expression system for protein synthesis due to their inherent superior secretory capabilities. The...

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Zhang Z, Xiang B, Zhao S, et al. Construction of a novel filamentous fungal protein expression system based on redesigning of regulatory elements. Appl Microbiol Biotechnol. 2022;106(2):647-661doi: 10.1007/s00253-022-11761-0.
Zhang, Z., Xiang, B., Zhao, S., Yang, L., Chen, Y., Hu, Y., & Hu, S. (2022). Construction of a novel filamentous fungal protein expression system based on redesigning of regulatory elements. Applied microbiology and biotechnology, 106(2), 647-661. https://doi.org/10.1007/s00253-022-11761-0
Zhang, Zhe, et al. "Construction of a novel filamentous fungal protein expression system based on redesigning of regulatory elements." Applied microbiology and biotechnology vol. 106,2 (2022): 647-661. doi: https://doi.org/10.1007/s00253-022-11761-0
Zhang Z, Xiang B, Zhao S, Yang L, Chen Y, Hu Y, Hu S. Construction of a novel filamentous fungal protein expression system based on redesigning of regulatory elements. Appl Microbiol Biotechnol. 2022 Jan;106(2):647-661. doi: 10.1007/s00253-022-11761-0. Epub 2022 Jan 12. PMID: 35019997.
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An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification.

Biotechnology for biofuels

Corrêa TLR, Júnior AT, Wolf LD, Buckeridge MS, Dos Santos LV, Murakami MT.
PMID: 31168322
Biotechnol Biofuels. 2019 May 10;12:117. doi: 10.1186/s13068-019-1449-0. eCollection 2019.

BACKGROUND: Lytic polysaccharide monooxygenases (LPMOs) opened a new horizon for biomass deconstruction. They use a redox mechanism not yet fully understood and the range of substrates initially envisaged to be the crystalline polysaccharides is steadily expanding to non-crystalline ones.RESULTS:...

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Corrêa TLR, Júnior AT, Wolf LD, et al. An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification. Biotechnol Biofuels. 2019;12:117doi: 10.1186/s13068-019-1449-0.
Corrêa, T. L. R., Júnior, A. T., Wolf, L. D., Buckeridge, M. S., Dos Santos, L. V., & Murakami, M. T. (2019). An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification. Biotechnology for biofuels, 12117. https://doi.org/10.1186/s13068-019-1449-0
Corrêa, Thamy Lívia Ribeiro, et al. "An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification." Biotechnology for biofuels vol. 12 (2019): 117. doi: https://doi.org/10.1186/s13068-019-1449-0
Corrêa TLR, Júnior AT, Wolf LD, Buckeridge MS, Dos Santos LV, Murakami MT. An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification. Biotechnol Biofuels. 2019 May 10;12:117. doi: 10.1186/s13068-019-1449-0. eCollection 2019. PMID: 31168322; PMCID: PMC6509861.
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Comparative molecular dynamics simulations identify a salt-sensitive loop responsible for the halotolerant activity of GH5 cellulases.

Journal of biomolecular structure & dynamics

Song Y, Wu X, Zhao Y, Jiang X, Wang L.
PMID: 34043936
J Biomol Struct Dyn. 2021 May 27;1-11. doi: 10.1080/07391102.2021.1930167. Epub 2021 May 27.

Halotolerant glycoside hydrolases (GH) have broad application potentials in biorefinery industries. Elucidating the structure-activity relationship underlying the halotolerant catalysis is essential to design superior biocatalysts. Here, we performed molecular dynamics simulations to investigate the structural dynamics of two GH5...

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Song Y, Wu X, Zhao Y, et al. Comparative molecular dynamics simulations identify a salt-sensitive loop responsible for the halotolerant activity of GH5 cellulases. J Biomol Struct Dyn. 2021;1-11doi: 10.1080/07391102.2021.1930167.
Song, Y., Wu, X., Zhao, Y., Jiang, X., & Wang, L. (2021). Comparative molecular dynamics simulations identify a salt-sensitive loop responsible for the halotolerant activity of GH5 cellulases. Journal of biomolecular structure & dynamics, 1-11. https://doi.org/10.1080/07391102.2021.1930167
Song, Yuxuan, et al. "Comparative molecular dynamics simulations identify a salt-sensitive loop responsible for the halotolerant activity of GH5 cellulases." Journal of biomolecular structure & dynamics vol. (2021): 1-11. doi: https://doi.org/10.1080/07391102.2021.1930167
Song Y, Wu X, Zhao Y, Jiang X, Wang L. Comparative molecular dynamics simulations identify a salt-sensitive loop responsible for the halotolerant activity of GH5 cellulases. J Biomol Struct Dyn. 2021 May 27;1-11. doi: 10.1080/07391102.2021.1930167. Epub 2021 May 27. PMID: 34043936.
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Succession of Gut Microbial Structure in Twin Giant Pandas During the Dietary Change Stage and Its Role in Polysaccharide Metabolism.

Frontiers in microbiology

Zhan M, Wang L, Xie C, Fu X, Zhang S, Wang A, Zhou Y, Xu C, Zhang H.
PMID: 33072012
Front Microbiol. 2020 Sep 22;11:551038. doi: 10.3389/fmicb.2020.551038. eCollection 2020.

Adaptation to a bamboo diet is an essential process for giant panda growth, and gut microbes play an important role in the digestion of the polysaccharides in bamboo. The dietary transition in giant panda cubs is particularly complex, but...

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Zhan M, Wang L, Xie C, et al. Succession of Gut Microbial Structure in Twin Giant Pandas During the Dietary Change Stage and Its Role in Polysaccharide Metabolism. Front Microbiol. 2020;11:551038doi: 10.3389/fmicb.2020.551038.
Zhan, M., Wang, L., Xie, C., Fu, X., Zhang, S., Wang, A., Zhou, Y., Xu, C., & Zhang, H. (2020). Succession of Gut Microbial Structure in Twin Giant Pandas During the Dietary Change Stage and Its Role in Polysaccharide Metabolism. Frontiers in microbiology, 11551038. https://doi.org/10.3389/fmicb.2020.551038
Zhan, Mingye, et al. "Succession of Gut Microbial Structure in Twin Giant Pandas During the Dietary Change Stage and Its Role in Polysaccharide Metabolism." Frontiers in microbiology vol. 11 (2020): 551038. doi: https://doi.org/10.3389/fmicb.2020.551038
Zhan M, Wang L, Xie C, Fu X, Zhang S, Wang A, Zhou Y, Xu C, Zhang H. Succession of Gut Microbial Structure in Twin Giant Pandas During the Dietary Change Stage and Its Role in Polysaccharide Metabolism. Front Microbiol. 2020 Sep 22;11:551038. doi: 10.3389/fmicb.2020.551038. eCollection 2020. PMID: 33072012; PMCID: PMC7537565.
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Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium .

PeerJ

Furusawa G, Azami NA, Teh AH.
PMID: 33732545
PeerJ. 2021 Mar 09;9:e10929. doi: 10.7717/peerj.10929. eCollection 2021.

BACKGROUND: Oligosaccharides from polysaccharides containing uronic acids are known to have many useful bioactivities. Thus, polysaccharide lyases (PLs) and glycoside hydrolases (GHs) involved in producing the oligosaccharides have attracted interest in both medical and industrial settings. The numerous polysaccharide...

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Furusawa G, Azami NA, Teh AH. Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium . PeerJ. 2021;9:e10929doi: 10.7717/peerj.10929.
Furusawa, G., Azami, N. A., & Teh, A. H. (2021). Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium . PeerJ, 9e10929. https://doi.org/10.7717/peerj.10929
Furusawa, Go, et al. "Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium ." PeerJ vol. 9 (2021): e10929. doi: https://doi.org/10.7717/peerj.10929
Furusawa G, Azami NA, Teh AH. Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium . PeerJ. 2021 Mar 09;9:e10929. doi: 10.7717/peerj.10929. eCollection 2021. PMID: 33732545; PMCID: PMC7953866.
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Enhanced production of ginsenoside Rh2(.

Saudi journal of biological sciences

Siddiqi MZ, Ximenes HA, Song BK, Park HY, Lee WH, Han H, Im WT.
PMID: 34354454
Saudi J Biol Sci. 2021 Aug;28(8):4668-4676. doi: 10.1016/j.sjbs.2021.04.079. Epub 2021 May 01.

BACKGROUND: Ginsenoside Rh2(METHOD: Three glycoside hydrolases (BglBX10, Abf22-3, and BglSk) were cloned in RESULTS: The designed bioconversion pathways show that Abf22-3 and BglBX10 were responsible for the conversion of Rb1, Rc and Rd → Rg3(CONCLUSION: Our pilot data demonstrate...

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Siddiqi MZ, Ximenes HA, Song BK, et al. Enhanced production of ginsenoside Rh2(. Saudi J Biol Sci. 2021;28(8):4668-4676doi: 10.1016/j.sjbs.2021.04.079.
Siddiqi, M. Z., Ximenes, H. A., Song, B. K., Park, H. Y., Lee, W. H., Han, H., & Im, W. T. (2021). Enhanced production of ginsenoside Rh2(. Saudi journal of biological sciences, 28(8), 4668-4676. https://doi.org/10.1016/j.sjbs.2021.04.079
Siddiqi, Muhammad Zubair, et al. "Enhanced production of ginsenoside Rh2(." Saudi journal of biological sciences vol. 28,8 (2021): 4668-4676. doi: https://doi.org/10.1016/j.sjbs.2021.04.079
Siddiqi MZ, Ximenes HA, Song BK, Park HY, Lee WH, Han H, Im WT. Enhanced production of ginsenoside Rh2(. Saudi J Biol Sci. 2021 Aug;28(8):4668-4676. doi: 10.1016/j.sjbs.2021.04.079. Epub 2021 May 01. PMID: 34354454; PMCID: PMC8324944.
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Showing 25 to 36 of 222 entries