LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Back to previous search Search history
Advanced search

Your last searches

  1. AU="Canova, Christopher T"
  2. AU="Hasnaoui, Naoual"
  3. AU="Maradana, Jhansi"
  4. AU="Raggini, Elisa"
  5. AU="Baxter, A."
  6. AU="Jackson, Shirnae"
  7. AU="Schenzle, Lisa"
  8. AU="Veronica Phillips"
  9. AU="Braun, Jörg"
  10. AU="Cassandra E. Holbert"
  11. AU="Trevisan Alexandra"

Search results

Result 1 - 3 of total 3

Search options

  1. Article ; Online: Mechanistic modeling of viral particle production.

    Canova, Christopher T / Inguva, Pavan K / Braatz, Richard D

    Biotechnology and bioengineering

    2022  Volume 120, Issue 3, Page(s) 629–641

    Abstract: Viral systems such as wild-type viruses, viral vectors, and virus-like particles are essential components of modern biotechnology and medicine. Despite their importance, the commercial-scale production of viral systems remains highly inefficient for ... ...

    Abstract Viral systems such as wild-type viruses, viral vectors, and virus-like particles are essential components of modern biotechnology and medicine. Despite their importance, the commercial-scale production of viral systems remains highly inefficient for multiple reasons. Computational strategies are a promising avenue for improving process development, optimization, and control, but require a mathematical description of the system. This article reviews mechanistic modeling strategies for the production of viral particles, both at the cellular and bioreactor scales. In many cases, techniques and models from adjacent fields such as epidemiology and wild-type viral infection kinetics can be adapted to construct a suitable process model. These process models can then be employed for various purposes such as in-silico testing of novel process operating strategies and/or advanced process control.
    MeSH term(s) Humans ; Biotechnology/methods ; Bioreactors ; Virus Diseases ; Virion
    Language English
    Publishing date 2022-12-22
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.28296
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.B 960: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Analysis of Poly(ethylene terephthalate) degradation kinetics of evolved IsPETase variants using a surface crowding model.

    Zhong-Johnson, En Ze Linda / Dong, Ziyue / Canova, Christopher T / Destro, Francesco / Cañellas, Marina / Hoffman, Mikaila C / Maréchal, Jeanne / Johnson, Timothy M / Zheng, Maya / Schlau-Cohen, Gabriela S / Lucas, Maria Fátima / Braatz, Richard D / Sprenger, Kayla G / Voigt, Christopher A / Sinskey, Anthony J

    The Journal of biological chemistry

    2024  Volume 300, Issue 3, Page(s) 105783

    Abstract: Poly(ethylene terephthalate) (PET) is a major plastic polymer utilized in the single-use and textile industries. The discovery of PET-degrading enzymes (PETases) has led to an increased interest in the biological recycling of PET in addition to ... ...

    Abstract Poly(ethylene terephthalate) (PET) is a major plastic polymer utilized in the single-use and textile industries. The discovery of PET-degrading enzymes (PETases) has led to an increased interest in the biological recycling of PET in addition to mechanical recycling. IsPETase from Ideonella sakaiensis is a candidate catalyst, but little is understood about its structure-function relationships with regards to PET degradation. To understand the effects of mutations on IsPETase productivity, we develop a directed evolution assay to identify mutations beneficial to PET film degradation at 30 °C. IsPETase also displays enzyme concentration-dependent inhibition effects, and surface crowding has been proposed as a causal phenomenon. Based on total internal reflectance fluorescence microscopy and adsorption experiments, IsPETase is likely experiencing crowded conditions on PET films. Molecular dynamics simulations of IsPETase variants reveal a decrease in active site flexibility in free enzymes and reduced probability of productive active site formation in substrate-bound enzymes under crowding. Hence, we develop a surface crowding model to analyze the biochemical effects of three hit mutations (T116P, S238N, S290P) that enhanced ambient temperature activity and/or thermostability. We find that T116P decreases susceptibility to crowding, resulting in higher PET degradation product accumulation despite no change in intrinsic catalytic rate. In conclusion, we show that a macromolecular crowding-based biochemical model can be used to analyze the effects of mutations on properties of PETases and that crowding behavior is a major property to be targeted for enzyme engineering for improved PET degradation.
    MeSH term(s) Hydrolases/chemistry ; Hydrolases/genetics ; Hydrolases/metabolism ; Polyethylene Terephthalates/chemistry ; Polyethylene Terephthalates/metabolism ; Recycling ; Kinetics ; Burkholderiales/enzymology ; Models, Chemical
    Chemical Substances Hydrolases (EC 3.-) ; Polyethylene Terephthalates
    Language English
    Publishing date 2024-02-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.105783
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Correction: Analysis of Poly(ethylene terephthalate) degradation kinetics of evolved IsPETase variants using a surface crowding mode.

    Linda Zhong-Johnson, En Ze / Dong, Ziyue / Canova, Christopher T / Destro, Francesco / Cañellas, Marina / Hoffman, Mikaila C / Maréchal, Jeanne / Johnson, Timothy M / Zheng, Maya / Schlau-Cohen, Gabriela S / Lucas, Maria Fátima / Braatz, Richard D / Sprenger, Kayla G / Voigt, Christopher A / Sinskey, Anthony J

    The Journal of biological chemistry

    2024  Volume 300, Issue 4, Page(s) 107240

    Language English
    Publishing date 2024-04-04
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.107240
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top