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  1. Artikel ; Online: Continuous culture of anaerobic fungi enables growth and metabolic flux tuning without use of genetic tools.

    Leggieri, Patrick A / Blair, Elaina M / Lankiewicz, Thomas S / O'Malley, Michelle A

    Bioresource technology

    2023  Band 391, Heft Pt A, Seite(n) 129854

    Abstract: Anaerobic gut fungi (AGF) have potential to valorize lignocellulosic biomass owing to their diverse repertoire of carbohydrate-active enzymes (CAZymes). However, AGF metabolism is poorly understood, and no stable genetic tools are available to manipulate ...

    Abstract Anaerobic gut fungi (AGF) have potential to valorize lignocellulosic biomass owing to their diverse repertoire of carbohydrate-active enzymes (CAZymes). However, AGF metabolism is poorly understood, and no stable genetic tools are available to manipulate growth and metabolic flux to enhance production of specific targets, e.g., cells, CAZymes, or metabolites. Herein, a cost-effective, Arduino-based, continuous-flow anaerobic bioreactor with online optical density control is presented to probe metabolism and predictably tune fluxes in Caecomyces churrovis. Varying the C. churrovis turbidostat setpoint titer reliably controlled growth rate (from 0.04 to 0.20 h
    Mesh-Begriff(e) Fermentation ; Anaerobiosis ; Acetates ; Lactates ; Formates/metabolism ; Ethanol/metabolism ; Fungi/metabolism
    Chemische Substanzen Acetates ; Lactates ; Formates ; Ethanol (3K9958V90M)
    Sprache Englisch
    Erscheinungsdatum 2023-10-18
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1065195-0
    ISSN 1873-2976 ; 0960-8524
    ISSN (online) 1873-2976
    ISSN 0960-8524
    DOI 10.1016/j.biortech.2023.129854
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Microbial communities and their enzymes facilitate degradation of recalcitrant polymers in anaerobic digestion.

    Blair, Elaina M / Dickson, Katharine L / O'Malley, Michelle A

    Current opinion in microbiology

    2021  Band 64, Seite(n) 100–108

    Abstract: Microbial consortia efficiently degrade complex biopolymers found in the organic fraction of municipal solid waste (OFMSW). Through enzyme production and division of labor during anaerobic digestion, microbial communities break down recalcitrant polymers ...

    Abstract Microbial consortia efficiently degrade complex biopolymers found in the organic fraction of municipal solid waste (OFMSW). Through enzyme production and division of labor during anaerobic digestion, microbial communities break down recalcitrant polymers and make fermentation products, including methane. However, microbial communities remain underutilized for waste degradation as it remains difficult to characterize and predict microbial interactions during waste breakdown, especially as cultivation conditions change drastically throughout anaerobic digestion. This review discusses recent progress and opportunities in cultivating natural and engineered consortia for OFMSW hydrolysis, including how recalcitrant substrates are degraded by enzymes as well as the critical factors that govern microbial interactions and culture stability. Methods to measure substrate degradation are also reviewed, and we demonstrate the need for increased standardization to enable comparisons across different environments.
    Mesh-Begriff(e) Anaerobiosis ; Bioreactors ; Microbiota ; Polymers ; Refuse Disposal
    Chemische Substanzen Polymers
    Sprache Englisch
    Erscheinungsdatum 2021-10-23
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2021.09.008
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel: Microbial communities and their enzymes facilitate degradation of recalcitrant polymers in anaerobic digestion

    Blair, Elaina M / Dickson, Katharine L / O’Malley, Michelle A

    Current opinion in microbiology. 2021 Dec., v. 64

    2021  

    Abstract: Microbial consortia efficiently degrade complex biopolymers found in the organic fraction of municipal solid waste (OFMSW). Through enzyme production and division of labor during anaerobic digestion, microbial communities break down recalcitrant polymers ...

    Abstract Microbial consortia efficiently degrade complex biopolymers found in the organic fraction of municipal solid waste (OFMSW). Through enzyme production and division of labor during anaerobic digestion, microbial communities break down recalcitrant polymers and make fermentation products, including methane. However, microbial communities remain underutilized for waste degradation as it remains difficult to characterize and predict microbial interactions during waste breakdown, especially as cultivation conditions change drastically throughout anaerobic digestion. This review discusses recent progress and opportunities in cultivating natural and engineered consortia for OFMSW hydrolysis, including how recalcitrant substrates are degraded by enzymes as well as the critical factors that govern microbial interactions and culture stability. Methods to measure substrate degradation are also reviewed, and we demonstrate the need for increased standardization to enable comparisons across different environments.
    Schlagwörter anaerobic digestion ; biopolymers ; enzymes ; fermentation ; hydrolysis ; labor ; methane ; microbiology ; municipal solid waste
    Sprache Englisch
    Erscheinungsverlauf 2021-12
    Umfang p. 100-108.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2021.09.008
    Datenquelle NAL Katalog (AGRICOLA)

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  4. Artikel ; Online: Pontiella agarivorans

    Liu, Na / Kivenson, Veronika / Peng, Xuefeng / Cui, Zhisong / Lankiewicz, Thomas S / Gosselin, Kelsey M / English, Chance J / Blair, Elaina M / O'Malley, Michelle A / Valentine, David L

    Applied and environmental microbiology

    2024  Band 90, Heft 2, Seite(n) e0091423

    Abstract: Marine macroalgae produce abundant and diverse polysaccharides, which contribute substantially to the organic matter exported to the deep ocean. Microbial degradation of these polysaccharides plays an important role in the turnover of macroalgal biomass. ...

    Abstract Marine macroalgae produce abundant and diverse polysaccharides, which contribute substantially to the organic matter exported to the deep ocean. Microbial degradation of these polysaccharides plays an important role in the turnover of macroalgal biomass. Various members of the
    Mesh-Begriff(e) Anaerobiosis ; Base Composition ; RNA, Ribosomal, 16S/genetics ; RNA, Ribosomal, 16S/metabolism ; Phylogeny ; Sequence Analysis, DNA ; Bacteria, Anaerobic/metabolism ; Polysaccharides/metabolism ; Alteromonadaceae/genetics ; Carrageenan ; DNA, Bacterial/analysis ; Fatty Acids ; Bacterial Typing Techniques
    Chemische Substanzen RNA, Ribosomal, 16S ; Polysaccharides ; Carrageenan (9000-07-1) ; DNA, Bacterial ; Fatty Acids
    Sprache Englisch
    Erscheinungsdatum 2024-01-24
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/aem.00914-23
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Improved soluble expression and use of recombinant human renalase.

    Morrison, Clifford S / Paskaleva, Elena E / Rios, Marvin A / Beusse, Thomas R / Blair, Elaina M / Lin, Lucy Q / Hu, James R / Gorby, Aidan H / Dodds, David R / Armiger, William B / Dordick, Jonathan S / Koffas, Mattheos A G

    PloS one

    2020  Band 15, Heft 11, Seite(n) e0242109

    Abstract: Electrochemical bioreactor systems have enjoyed significant attention in the past few decades, particularly because of their applications to biobatteries, artificial photosynthetic systems, and microbial electrosynthesis. A key opportunity with ... ...

    Abstract Electrochemical bioreactor systems have enjoyed significant attention in the past few decades, particularly because of their applications to biobatteries, artificial photosynthetic systems, and microbial electrosynthesis. A key opportunity with electrochemical bioreactors is the ability to employ cofactor regeneration strategies critical in oxidative and reductive enzymatic and cell-based biotransformations. Electrochemical cofactor regeneration presents several advantages over other current cofactor regeneration systems, such as chemoenzymatic multi-enzyme reactions, because there is no need for a sacrificial substrate and a recycling enzyme. Additionally, process monitoring is simpler and downstream processing is less costly. However, the direct electrochemical reduction of NAD(P)+ on a cathode may produce adventitious side products, including isomers of NAD(P)H that can act as potent competitive inhibitors to NAD(P)H-requiring enzymes such as dehydrogenases. To overcome this limitation, we examined how nature addresses the adventitious formation of isomers of NAD(P)H. Specifically, renalases are enzymes that catalyze the oxidation of 1,2- and 1,6-NAD(P)H to NAD(P)+, yielding an effective recycling of unproductive NAD(P)H isomers. We designed several mutants of recombinant human renalase isoform 1 (rhRen1), expressed them in E. coli BL21(DE3) to enhance protein solubility, and evaluated the activity profiles of the renalase variants against NAD(P)H isomers. The potential for rhRen1 to be employed in engineering applications was then assessed in view of the enzyme's stability upon immobilization. Finally, comparative modeling was performed to assess the underlying reasons for the enhanced solubility and activity of the mutant enzymes.
    Mesh-Begriff(e) Enzyme Stability ; Escherichia coli ; Humans ; Industrial Microbiology/methods ; Monoamine Oxidase/chemistry ; Monoamine Oxidase/genetics ; Monoamine Oxidase/metabolism ; Mutation ; NADP/metabolism ; Protein Domains ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Solubility ; Static Electricity
    Chemische Substanzen Recombinant Proteins ; NADP (53-59-8) ; Monoamine Oxidase (EC 1.4.3.4) ; renalase (EC 1.4.3.4.)
    Sprache Englisch
    Erscheinungsdatum 2020-11-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0242109
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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