Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes

Research output: Contribution to journal › Journal article › Research › peer-review

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Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes. / Guo, Rui-Rui; Comamala, Gerard; Yang, Huan-Huan; Gramlich, Marius; Du, Ya-Min; Wang, Ting; Zeck, Anne; Rand, Kasper Dyrberg; Liu, Li; Voglmeir, Josef.

In: Frontiers in Bioengineering and Biotechnology, Vol. 8, 741, 2020.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Guo, R-R, Comamala, G, Yang, H-H, Gramlich, M, Du, Y-M, Wang, T, Zeck, A, Rand, KD, Liu, L & Voglmeir, J 2020, 'Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes', Frontiers in Bioengineering and Biotechnology, vol. 8, 741. https://doi.org/10.3389/fbioe.2020.00741

APA

Guo, R-R., Comamala, G., Yang, H-H., Gramlich, M., Du, Y-M., Wang, T., Zeck, A., Rand, K. D., Liu, L., & Voglmeir, J. (2020). Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes. Frontiers in Bioengineering and Biotechnology, 8, [741]. https://doi.org/10.3389/fbioe.2020.00741

Vancouver

Guo R-R, Comamala G, Yang H-H, Gramlich M, Du Y-M, Wang T et al. Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes. Frontiers in Bioengineering and Biotechnology. 2020;8. 741. https://doi.org/10.3389/fbioe.2020.00741

Author

Guo, Rui-Rui ; Comamala, Gerard ; Yang, Huan-Huan ; Gramlich, Marius ; Du, Ya-Min ; Wang, Ting ; Zeck, Anne ; Rand, Kasper Dyrberg ; Liu, Li ; Voglmeir, Josef. / Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes. In: Frontiers in Bioengineering and Biotechnology. 2020 ; Vol. 8.

Bibtex

@article{959c05b9f7ae46bdafe39a97ab8c10e2,
title = "Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes",
abstract = "Peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidases (PNGases, N-glycanases, EC 3.5.1.52) are indispensable tools in releasing N-glycans from glycoproteins. So far, only a limited number of PNGase candidates are available for the structural analysis of glycoproteins and their glycan moieties. Herein, a panel of 13 novel PNGase H+ candidates (the suffix H+ refers to the acidic pH optimum of these acidobacterial PNGases) was tested in their recombinant form for their deglycosylation performance. One candidate (originating from the bacterial species Dyella japonica) showed superior properties both in solution-phase and immobilized on amino-, epoxy- and nitrilotriacetate resins when compared to currently acidic available PNGases. The high expression yield compared to a previously described PNGase H+, broad substrate specificity, and good storage stability of this novel N-glycanase makes it a valuable tool for the analysis of protein glycosylation.",
author = "Rui-Rui Guo and Gerard Comamala and Huan-Huan Yang and Marius Gramlich and Ya-Min Du and Ting Wang and Anne Zeck and Rand, {Kasper Dyrberg} and Li Liu and Josef Voglmeir",
note = "Copyright {\textcopyright} 2020 Guo, Comamala, Yang, Gramlich, Du, Wang, Zeck, Rand, Liu and Voglmeir.",
year = "2020",
doi = "10.3389/fbioe.2020.00741",
language = "English",
volume = "8",
journal = "Frontiers in Bioengineering and Biotechnology",
issn = "2296-4185",
publisher = "Frontiers Media",

}

RIS

TY - JOUR

T1 - Discovery of Highly Active Recombinant PNGase H+ Variants Through the Rational Exploration of Unstudied Acidobacterial Genomes

AU - Guo, Rui-Rui

AU - Comamala, Gerard

AU - Yang, Huan-Huan

AU - Gramlich, Marius

AU - Du, Ya-Min

AU - Wang, Ting

AU - Zeck, Anne

AU - Rand, Kasper Dyrberg

AU - Liu, Li

AU - Voglmeir, Josef

N1 - Copyright © 2020 Guo, Comamala, Yang, Gramlich, Du, Wang, Zeck, Rand, Liu and Voglmeir.

PY - 2020

Y1 - 2020

N2 - Peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidases (PNGases, N-glycanases, EC 3.5.1.52) are indispensable tools in releasing N-glycans from glycoproteins. So far, only a limited number of PNGase candidates are available for the structural analysis of glycoproteins and their glycan moieties. Herein, a panel of 13 novel PNGase H+ candidates (the suffix H+ refers to the acidic pH optimum of these acidobacterial PNGases) was tested in their recombinant form for their deglycosylation performance. One candidate (originating from the bacterial species Dyella japonica) showed superior properties both in solution-phase and immobilized on amino-, epoxy- and nitrilotriacetate resins when compared to currently acidic available PNGases. The high expression yield compared to a previously described PNGase H+, broad substrate specificity, and good storage stability of this novel N-glycanase makes it a valuable tool for the analysis of protein glycosylation.

AB - Peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidases (PNGases, N-glycanases, EC 3.5.1.52) are indispensable tools in releasing N-glycans from glycoproteins. So far, only a limited number of PNGase candidates are available for the structural analysis of glycoproteins and their glycan moieties. Herein, a panel of 13 novel PNGase H+ candidates (the suffix H+ refers to the acidic pH optimum of these acidobacterial PNGases) was tested in their recombinant form for their deglycosylation performance. One candidate (originating from the bacterial species Dyella japonica) showed superior properties both in solution-phase and immobilized on amino-, epoxy- and nitrilotriacetate resins when compared to currently acidic available PNGases. The high expression yield compared to a previously described PNGase H+, broad substrate specificity, and good storage stability of this novel N-glycanase makes it a valuable tool for the analysis of protein glycosylation.

U2 - 10.3389/fbioe.2020.00741

DO - 10.3389/fbioe.2020.00741

M3 - Journal article

C2 - 32719787

VL - 8

JO - Frontiers in Bioengineering and Biotechnology

JF - Frontiers in Bioengineering and Biotechnology

SN - 2296-4185

M1 - 741

ER -

ID: 246668637