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  1. AU="Sana, Barindra"
  2. AU="Hoepken, Bengt"
  3. AU="Crossman, Kerryn"
  4. AU="Mendonça, Halysson B"
  5. AU="Rodenstein, Daniel Oscar"
  6. AU="Csont, Tamás"
  7. AU="Yusuf, Qamar Kassim"
  8. AU="Izquierdo-Vega, Judith"
  9. AU="Barc, Céline"
  10. AU="Herath, Tharuka"
  11. AU="Klontz, Erik H"
  12. AU=Lu Chen Chen
  13. AU="Shabsovich, David"
  14. AU="Foraker, Randi E"
  15. AU="Kolonko, Aureliusz"
  16. AU=Falagas M E
  17. AU="Dunstan, Melanie L"
  18. AU=Kacar Mark AU=Kacar Mark
  19. AU="Schaup, Rebecca Michaela"
  20. AU="Ye, Chaofu"
  21. AU="Tekin, Nur"
  22. AU="Martens, Dirk E"
  23. AU=Teos Leyla Y.
  24. AU="Sánchez-Garcia, Joaquín"
  25. AU="Schaller, Benoit"
  26. AU="Hernandez, A"
  27. AU="Nguyen, Thien H"
  28. AU="Park, Jung Wan"
  29. AU="Mahajan, Aman"
  30. AU="Hao, Yanling"
  31. AU="Eing, Lorenz"
  32. AU="Geoffroy, Pierre A"
  33. AU="Chapuis, J"
  34. AU="Berta, László"
  35. AU="Barzilay, Regina"
  36. AU="Schmidt, Michael Rahbek"
  37. AU=Tack J
  38. AU="Oh, Hye Min"
  39. AU=Gaffen Sarah L AU=Gaffen Sarah L
  40. AU="Schmitt, Christine"
  41. AU="McKay, Jackie"
  42. AU="Bellissimo, Catherine A"
  43. AU="Desai, Urja"
  44. AU="Chini, Maria Giovanna"
  45. AU="Xiao, Difei"
  46. AU="Ryan, Chris"
  47. AU="Omar Bazighifan"
  48. AU="Corominas Galbany, Jordi"
  49. AU=Fox Norma E
  50. AU="Hamilton, Shelia M"
  51. AU="Nichols, J Wylie"
  52. AU="Pesce R."
  53. AU="Gambitta, P"
  54. AU="Imran, Aqeel"
  55. AU="Sharma, Yashoda"
  56. AU="Kosai, Jordyn"
  57. AU="Aroca Ferri, María"
  58. AU="Laba, Stephanie"
  59. AU="Kim, Ye-Sel"

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Treffer 1 - 10 von insgesamt 26

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  1. Artikel: Bioresources for control of environmental pollution.

    Sana, Barindra

    Advances in biochemical engineering/biotechnology

    2015  Band 147, Seite(n) 137–183

    Abstract: Environmental pollution is one of the biggest threats to human beings. For practical reasons it is not possible to stop most of the activities responsible for environmental pollution; rather we need to eliminate the pollutants. In addition to other ... ...

    Abstract Environmental pollution is one of the biggest threats to human beings. For practical reasons it is not possible to stop most of the activities responsible for environmental pollution; rather we need to eliminate the pollutants. In addition to other existing means, biological processes can be utilized to get rid of toxic pollutants. Degradation, removal, or deactivation of pollutants by biological means is known as bioremediation. Nature itself has several weapons to deal with natural wastage and some of them are equally active for eliminating nonnatural pollutants. Several plants, microorganisms, and some lower eukaryotes utilize environmental pollutants as nutrients and some of them are very efficient for decontaminating specific types of pollutants. If exploited properly, these natural resources have enough potential to deal with most elements of environmental pollution. In addition, several artificial microbial consortia and genetically modified organisms with high bioremediation potential were developed by application of advanced scientific tools. On the other hand, natural equilibria of ecosystems are being affected by human intervention. Rapid population growth, urbanization, and industrialization are destroying ecological balances and the natural remediation ability of the Earth is being compromised. Several potential bioremediation tools are also being destroyed by biodiversity destruction of unexplored ecosystems. Pollution management by bioremediation is highly dependent on abundance, exploration, and exploitation of bioresources, and biodiversity is the key to success. Better pollution management needs the combined actions of biodiversity conservation, systematic exploration of natural resources, and their exploitation with sophisticated modern technologies.
    Mesh-Begriff(e) Bacteria/metabolism ; Biodegradation, Environmental ; Biodiversity ; Conservation of Natural Resources/methods ; Environmental Pollutants/isolation & purification ; Environmental Pollutants/metabolism ; Environmental Pollution/prevention & control ; Plants/metabolism
    Chemische Substanzen Environmental Pollutants
    Sprache Englisch
    Erscheinungsdatum 2015
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ISSN 0724-6145
    ISSN 0724-6145
    DOI 10.1007/10_2014_276
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: The influences of substrates' physical properties on enzymatic PET hydrolysis: Implications for PET hydrolase engineering.

    Pasula, Rupali Reddy / Lim, Sierin / Ghadessy, Farid J / Sana, Barindra

    Engineering biology

    2022  Band 6, Heft 1, Seite(n) 17–22

    Abstract: Plastic pollution in diverse terrestrial and marine environments is a widely recognised and growing problem. Bio-recycling and upcycling of plastic waste is a potential solution to plastic pollution, as these processes convert plastic waste into useful ... ...

    Abstract Plastic pollution in diverse terrestrial and marine environments is a widely recognised and growing problem. Bio-recycling and upcycling of plastic waste is a potential solution to plastic pollution, as these processes convert plastic waste into useful materials. Polyethylene terephthalate (PET) is the most abundant plastic waste, and this material can be degraded by a class of recently discovered bacterial esterase enzymes known as PET hydrolases (PETase). Investigations of the enzymatic hydrolysis of diverse PET molecules have clearly revealed that the biodegradability of various PET substrates depends on both their chemical structure and physical properties, including polymer length, crystallinity, glass transition temperature, surface area, and surface charge. This review summarises the known impacts of crystallinity and other physical properties on enzymatic PET hydrolysis.
    Sprache Englisch
    Erscheinungsdatum 2022-03-24
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Review
    ISSN 2398-6182
    ISSN (online) 2398-6182
    DOI 10.1049/enb2.12018
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Halogenation of Peptides and Proteins Using Engineered Tryptophan Halogenase Enzymes.

    Sana, Barindra / Ke, Ding / Li, Eunice Hui Yen / Ho, Timothy / Seayad, Jayasree / Duong, Hung A / Ghadessy, Farid J

    Biomolecules

    2022  Band 12, Heft 12

    Abstract: Halogenation of bioactive peptides via incorporation of non-natural amino acid derivatives during chemical synthesis is a common strategy to enhance functionality. Bacterial tyrptophan halogenases efficiently catalyze regiospecific halogenation of the ... ...

    Abstract Halogenation of bioactive peptides via incorporation of non-natural amino acid derivatives during chemical synthesis is a common strategy to enhance functionality. Bacterial tyrptophan halogenases efficiently catalyze regiospecific halogenation of the free amino acid tryptophan, both in vitro and in vivo. Expansion of their substrate scope to peptides and proteins would facilitate highly-regulated post-synthesis/expression halogenation. Here, we demonstrate novel in vitro halogenation (chlorination and bromination) of peptides by select halogenase enzymes and identify the C-terminal (G/S)GW motif as a preferred substrate. In a first proof-of-principle experiment, we also demonstrate chemo-catalyzed derivatization of an enzymatically chlorinated peptide, albeit with low efficiency. We further rationally derive PyrH halogenase mutants showing improved halogenation of the (G/S)GW motif, both as a free peptide and when genetically fused to model proteins with efficiencies up to 90%.
    Sprache Englisch
    Erscheinungsdatum 2022-12-08
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom12121841
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Determining the relaxivity values of protein cage-templated nanoparticles using magnetic resonance imaging.

    Sana, Barindra / Lim, Sierin

    Methods in molecular biology (Clifton, N.J.)

    2015  Band 1252, Seite(n) 39–50

    Abstract: The application of magnetic resonance imaging (MRI) is often limited by low magnetic relaxivity of currently used contrast agents. This problem can be addressed by developing more sensitive contrast agents by synthesizing new types of metal complex or ... ...

    Abstract The application of magnetic resonance imaging (MRI) is often limited by low magnetic relaxivity of currently used contrast agents. This problem can be addressed by developing more sensitive contrast agents by synthesizing new types of metal complex or metallic nanoparticles. Protein cage has been used as a template in biological synthesis of magnetic nanoparticles. The magnetic nanoparticle-protein cage composites have been reported to have high magnetic relaxivity, which implies their potential application as an MRI contrast agent. The magnetic relaxivity is determined by measuring longitudinal and transverse magnetic relaxivities of the potential agent. The commonly performed techniques are field-cycling NMR relaxometry (also known as variable field relaxometry or nuclear magnetic relaxation dispersion (NMRD) profiling) and in vitro or in vivo MRI relaxometry. Here, we describe techniques for the synthesis of nanoparticle-protein cage composite and determination of their magnetic relaxivities by in vitro MR image acquisition and data processing. In this method, longitudinal and transverse relaxivities are calculated by measuring relaxation rates of water hydrogen nuclei at different nanoparticle-protein cage composite concentrations.
    Mesh-Begriff(e) Archaea/chemistry ; Ferritins/chemistry ; Magnetic Resonance Imaging ; Magnetite Nanoparticles/chemistry ; Magnetite Nanoparticles/ultrastructure ; Nanoparticles/chemistry ; Nanoparticles/ultrastructure ; Proteins/chemistry ; Sepharose/chemistry
    Chemische Substanzen Magnetite Nanoparticles ; Proteins ; Ferritins (9007-73-2) ; Sepharose (9012-36-6)
    Sprache Englisch
    Erscheinungsdatum 2015
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-2131-7_4
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Thermostability enhancement of polyethylene terephthalate degrading PETase using self- and nonself-ligating protein scaffolding approaches.

    Sana, Barindra / Ding, Ke / Siau, Jia Wei / Pasula, Rupali Reddy / Chee, Sharon / Kharel, Sharad / Lena, Jean-Baptise Henri / Goh, Eunice / Rajamani, Lakshminarayanan / Lam, Yeng Ming / Lim, Sierin / Ghadessy, John F

    Biotechnology and bioengineering

    2023  Band 120, Heft 11, Seite(n) 3200–3209

    Abstract: Polyethylene terephthalate (PET) hydrolase enzymes show promise for enzymatic PET degradation and green recycling of single-use PET vessels representing a major source of global pollution. Their full potential can be unlocked with enzyme engineering to ... ...

    Abstract Polyethylene terephthalate (PET) hydrolase enzymes show promise for enzymatic PET degradation and green recycling of single-use PET vessels representing a major source of global pollution. Their full potential can be unlocked with enzyme engineering to render activities on recalcitrant PET substrates commensurate with cost-effective recycling at scale. Thermostability is a highly desirable property in industrial enzymes, often imparting increased robustness and significantly reducing quantities required. To date, most engineered PET hydrolases show improved thermostability over their parental enzymes. Here, we report engineered thermostable variants of Ideonella sakaiensis PET hydrolase enzyme (IsPETase) developed using two scaffolding strategies. The first employed SpyCatcher-SpyTag technology to covalently cyclize IsPETase, resulting in increased thermostability that was concomitant with reduced turnover of PET substrates compared to native IsPETase. The second approach using a GFP-nanobody fusion protein (vGFP) as a scaffold yielded a construct with a melting temperature of 80°C. This was further increased to 85°C when a thermostable PETase variant (FAST PETase) was scaffolded into vGFP, the highest reported so far for an engineered PET hydrolase derived from IsPETase. Thermostability enhancement using the vGFP scaffold did not compromise activity on PET compared to IsPETase. These contrasting results highlight potential topological and dynamic constraints imposed by scaffold choice as determinants of enzyme activity.
    Sprache Englisch
    Erscheinungsdatum 2023-08-09
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.28523
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  6. Artikel ; Online: Functional display of bioactive peptides on the vGFP scaffold.

    Chee, Sharon Min Qi / Wongsantichon, Jantana / Yi, Lau Sze / Sana, Barindra / Frosi, Yuri / Robinson, Robert C / Ghadessy, Farid J

    Scientific reports

    2021  Band 11, Heft 1, Seite(n) 10127

    Abstract: Grafting bioactive peptides into recipient protein scaffolds can often increase their activities by conferring enhanced stability and cellular longevity. Here, we describe use of vGFP as a novel scaffold to display peptides. vGFP comprises GFP fused to a ...

    Abstract Grafting bioactive peptides into recipient protein scaffolds can often increase their activities by conferring enhanced stability and cellular longevity. Here, we describe use of vGFP as a novel scaffold to display peptides. vGFP comprises GFP fused to a bound high affinity Enhancer nanobody that potentiates its fluorescence. We show that peptides inserted into the linker region between GFP and the Enhancer are correctly displayed for on-target interaction, both in vitro and in live cells by pull-down, measurement of target inhibition and imaging analyses. This is further confirmed by structural studies highlighting the optimal display of a vGFP-displayed peptide bound to Mdm2, the key negative regulator of p53 that is often overexpressed in cancer. We also demonstrate a potential biosensing application of the vGFP scaffold by showing target-dependent modulation of intrinsic fluorescence. vGFP is relatively thermostable, well-expressed and inherently fluorescent. These properties make it a useful scaffold to add to the existing tool box for displaying peptides that can disrupt clinically relevant protein-protein interactions.
    Mesh-Begriff(e) Amino Acid Sequence ; Biosensing Techniques ; Cell Surface Display Techniques ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Humans ; Models, Molecular ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Protein Binding ; Protein Conformation ; Protein Interaction Mapping/methods ; Proto-Oncogene Proteins c-mdm2/chemistry ; Proto-Oncogene Proteins c-mdm2/metabolism ; Structure-Activity Relationship
    Chemische Substanzen Peptides ; Green Fluorescent Proteins (147336-22-9) ; MDM2 protein, human (EC 2.3.2.27) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27)
    Sprache Englisch
    Erscheinungsdatum 2021-05-12
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-89421-y
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Development and structural characterization of an engineered multi-copper oxidase reporter of protein-protein interactions.

    Sana, Barindra / Chee, Sharon M Q / Wongsantichon, Jantana / Raghavan, Sarada / Robinson, Robert C / Ghadessy, Farid J

    The Journal of biological chemistry

    2019  Band 294, Heft 17, Seite(n) 7002–7012

    Abstract: Protein-protein interactions (PPIs) are ubiquitous in almost all biological processes and are often corrupted in diseased states. A detailed understanding of PPIs is therefore key to understanding cellular physiology and can yield attractive therapeutic ... ...

    Abstract Protein-protein interactions (PPIs) are ubiquitous in almost all biological processes and are often corrupted in diseased states. A detailed understanding of PPIs is therefore key to understanding cellular physiology and can yield attractive therapeutic targets. Here, we describe the development and structural characterization of novel
    Mesh-Begriff(e) Amino Acid Sequence ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Kinetics ; Ligands ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Protein Binding ; Protein Conformation ; Protein Engineering ; Proto-Oncogene Proteins c-mdm2/metabolism ; Sequence Homology, Amino Acid
    Chemische Substanzen Escherichia coli Proteins ; Ligands ; Oxidoreductases (EC 1.-) ; copper oxidase (EC 1.16.-) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27)
    Sprache Englisch
    Erscheinungsdatum 2019-02-15
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA118.007141
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  8. Artikel: The unique self-assembly/disassembly property of Archaeoglobus fulgidus ferritin and its implications on molecular release from the protein cage

    Sana, Barindra / Eric Johnson / Sierin Lim

    BBA - General Subjects. 2015 Dec., v. 1850

    2015  

    Abstract: In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields due to the ... ...

    Abstract In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields due to the low-pH treatment. In contrast, Archaeoglobus fulgidus open-pore ferritin (AfFtn) and its closed-pore mutant (AfFtn-AA) are present as dimeric species in neutral buffers that self-assemble into cage-like structure upon addition of metal ions.To understand the iron-mediated self-assembly and ascorbate-mediated disassembly properties, we studied the iron binding and release profile of the AfFtn and AfFtn-AA, and the corresponding oligomerization of their subunits.Fe2+ binding and conversion to Fe3+ triggered the self-assembly of cage-like structures from dimeric species of AfFtn and AfFtn-AA subunits, while disassembly was induced by dissolving the iron core with reducing agents. The closed-pore AfFtn-AA has identical iron binding kinetics but lower iron release rates when compared to AfFtn. While the iron binding rate is proportional to Fe2+ concentration, the iron release rate can be controlled by varying ascorbate concentrations.The AfFtn and AfFtn-AA cages formed by iron mineralization could be disassembled by dissolving the iron core. The open-pores of AfFtn contribute to enhanced reductive iron release while the small channels located at the 3-fold symmetry axis (3-fold channels) are used for iron uptake.The iron-mediated self-assembly/disassembly property of AfFtn offers a new set of molecular trigger for formation and dissociation of the protein cage, which can potentially regulate uptake and release of molecular cargo from protein cages.
    Schlagwörter Archaeoglobus ; buffers ; dissociation ; encapsulation ; ferritin ; iron ; mineralization ; mutants ; oligomerization ; pH ; reducing agents
    Sprache Englisch
    Erscheinungsverlauf 2015-12
    Umfang p. 2544-2551.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ZDB-ID 840755-1
    ISSN 0304-4165
    ISSN 0304-4165
    DOI 10.1016/j.bbagen.2015.08.019
    Datenquelle NAL Katalog (AGRICOLA)

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  9. Artikel: The unique self-assembly/disassembly property of Archaeoglobus fulgidus ferritin and its implications on molecular release from the protein cage.

    Sana, Barindra / Johnson, Eric / Lim, Sierin

    Biochimica et biophysica acta

    2015  Band 1850, Heft 12, Seite(n) 2544–2551

    Abstract: Background: In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields ...

    Abstract Background: In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields due to the low-pH treatment. In contrast, Archaeoglobus fulgidus open-pore ferritin (AfFtn) and its closed-pore mutant (AfFtn-AA) are present as dimeric species in neutral buffers that self-assemble into cage-like structure upon addition of metal ions.
    Methods: To understand the iron-mediated self-assembly and ascorbate-mediated disassembly properties, we studied the iron binding and release profile of the AfFtn and AfFtn-AA, and the corresponding oligomerization of their subunits.
    Results: Fe(2+) binding and conversion to Fe(3+) triggered the self-assembly of cage-like structures from dimeric species of AfFtn and AfFtn-AA subunits, while disassembly was induced by dissolving the iron core with reducing agents. The closed-pore AfFtn-AA has identical iron binding kinetics but lower iron release rates when compared to AfFtn. While the iron binding rate is proportional to Fe(2+) concentration, the iron release rate can be controlled by varying ascorbate concentrations.
    Conclusion: The AfFtn and AfFtn-AA cages formed by iron mineralization could be disassembled by dissolving the iron core. The open-pores of AfFtn contribute to enhanced reductive iron release while the small channels located at the 3-fold symmetry axis (3-fold channels) are used for iron uptake.
    General significance: The iron-mediated self-assembly/disassembly property of AfFtn offers a new set of molecular trigger for formation and dissociation of the protein cage, which can potentially regulate uptake and release of molecular cargo from protein cages.
    Mesh-Begriff(e) Archaeoglobus fulgidus/metabolism ; Ascorbic Acid/metabolism ; Ferritins/metabolism ; Kinetics
    Chemische Substanzen Ferritins (9007-73-2) ; Ascorbic Acid (PQ6CK8PD0R)
    Sprache Englisch
    Erscheinungsdatum 2015-12
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagen.2015.08.019
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel: Ecological roles and biotechnological applications of marine and intertidal microbial biofilms.

    Mitra, Sayani / Sana, Barindra / Mukherjee, Joydeep

    Advances in biochemical engineering/biotechnology

    2014  Band 146, Seite(n) 163–205

    Abstract: This review is a retrospective of ecological effects of bioactivities produced by biofilms of surface-dwelling marine/intertidal microbes as well as of the industrial and environmental biotechnologies developed exploiting the knowledge of biofilm ... ...

    Abstract This review is a retrospective of ecological effects of bioactivities produced by biofilms of surface-dwelling marine/intertidal microbes as well as of the industrial and environmental biotechnologies developed exploiting the knowledge of biofilm formation. Some examples of significant interest pertaining to the ecological aspects of biofilm-forming species belonging to the Roseobacter clade include autochthonous bacteria from turbot larvae-rearing units with potential application as a probiotic as well as production of tropodithietic acid and indigoidine. Species of the Pseudoalteromonas genus are important examples of successful surface colonizers through elaboration of the AlpP protein and antimicrobial agents possessing broad-spectrum antagonistic activity against medical and environmental isolates. Further examples of significance comprise antiprotozoan activity of Pseudoalteromonas tunicata elicited by violacein, inhibition of fungal colonization, antifouling activities, inhibition of algal spore germination, and 2-n-pentyl-4-quinolinol production. Nitrous oxide, an important greenhouse gas, emanates from surface-attached microbial activity of marine animals. Marine and intertidal biofilms have been applied in the biotechnological production of violacein, phenylnannolones, and exopolysaccharides from marine and tropical intertidal environments. More examples of importance encompass production of protease, cellulase, and xylanase, melanin, and riboflavin. Antifouling activity of Bacillus sp. and application of anammox bacterial biofilms in bioremediation are described. Marine biofilms have been used as anodes and cathodes in microbial fuel cells. Some of the reaction vessels for biofilm cultivation reviewed are roller bottle, rotating disc bioreactor, polymethylmethacrylate conico-cylindrical flask, fixed bed reactor, artificial microbial mats, packed-bed bioreactors, and the Tanaka photobioreactor.
    Mesh-Begriff(e) Anti-Bacterial Agents/biosynthesis ; Bacterial Proteins/metabolism ; Bioelectric Energy Sources ; Biofilms/growth & development ; Bioreactors ; Biotechnology/instrumentation ; Biotechnology/methods ; Hydroxyquinolines/metabolism ; Indoles/metabolism ; Melanins/biosynthesis ; Piperidones/metabolism ; Pseudoalteromonas/metabolism ; Riboflavin/biosynthesis ; Roseobacter/metabolism ; Tropolone/analogs & derivatives ; Tropolone/metabolism
    Chemische Substanzen Anti-Bacterial Agents ; Bacterial Proteins ; Hydroxyquinolines ; Indoles ; Melanins ; Piperidones ; tropodithietic acid ; indigoidine (2435-59-8) ; Tropolone (7L6DL16P1T) ; violacein (QJH0DSQ3SG) ; Riboflavin (TLM2976OFR)
    Sprache Englisch
    Erscheinungsdatum 2014
    Erscheinungsland Germany
    Dokumenttyp Journal Article ; Review
    ISSN 0724-6145
    ISSN 0724-6145
    DOI 10.1007/10_2014_271
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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