Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Diana M. Mate"'
Autor:
Diana M. Mate, Miguel Alcalde
Publikováno v:
Microbial Biotechnology, Vol 10, Iss 6, Pp 1457-1467 (2017)
Summary Laccases are multicopper containing enzymes capable of performing one electron oxidation of a broad range of substrates. Using molecular oxygen as the final electron acceptor, they release only water as a by‐product, and as such, laccases a
Externí odkaz:
https://doaj.org/article/ed72a723651d4bf3b9ed2ae410449abd
Autor:
Xiaolin Dai, Diana M. Mate, Ulrich Glebe, Tayebeh Mirzaei Garakani, Andrea Körner, Ulrich Schwaneberg, Alexander Böker
Publikováno v:
Polymers, Vol 10, Iss 2, p 151 (2018)
Sortase A (SrtA) from Staphylococcus aureus has been often used for ligating a protein with other natural or synthetic compounds in recent years. Here we show that SrtA-mediated ligation (SML) is universally applicable for the linkage of two purely a
Externí odkaz:
https://doaj.org/article/11dc3fdf2c0d4afa8d615f95ffa093dc
Autor:
Ulrich Schwaneberg, Jasmin Eidner, Gaurao V. Dhoke, Ronny Martinez, Catalina Novoa, Patrick Lorenz, Diana M. Mate, Ruth Schwerdtfeger, Mehdi D. Davari, Thomas Haarmann, Felix Jakob, Martina Schreiter
Publikováno v:
ChemBioChem. 20:1458-1466
To date, commercial laccase preparations are used in the food, textile, and paper and pulp industries (mild pH). Laccases are attractive in the synthesis of dye molecules or oxidative lignin treatment, which take place at high pH (≥8.0). So far, on
Autor:
Diana M. Mate, Pere Clapés, Esther Sanchez-Freire, Đurđa Vasić-Rački, Yuyin Qi, Karel Hernández, Morana Česnik, Zvjezdana Findrik Blažević, José Berenguer, María Luisa del Pozo, Aurelio Hidalgo, Sandra Bosch, Jaime Quesada
Publikováno v:
Biblos-e Archivo. Repositorio Institucional de la UAM
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
The use of enzymes in industrial processes is often limited by the unavailability of biocatalysts with prolonged stability. Thermostable enzymes allow increased process temperature and thus higher substrate and product solubility, reuse of expensive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5655a8bfdeec6e4839d90bf98389848a
http://hdl.handle.net/10486/702405
http://hdl.handle.net/10486/702405
Publikováno v:
ACS Combinatorial Science. 20:203-211
Sortase-catalyzed ligations have emerged as powerful tools for the site-specific ligation of peptides and proteins in material science and biocatalysis. In this work, a directed sortase evolution strategy (SortEvolve) has been developed as a general
Publikováno v:
Chemical Communications. 54:11467-11470
Directed sortase A evolution yielded the variants R159G and D165Q/D186G/K196V with increased resistance (2.2-fold) and catalytic efficiency (6.3-fold) in 45% (v/v) dimethylsulfoxide. Interestingly, D165Q/D186G/K196V also showed an up to 4.7-fold incr
Autor:
Miguel Alcalde, Diana M. Mate
Publikováno v:
Microbial Biotechnology, Vol 10, Iss 6, Pp 1457-1467 (2017)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Microbial Biotechnology
Digital.CSIC. Repositorio Institucional del CSIC
instname
Microbial Biotechnology
Special Issue: Thematic Issue: From complex waste to plastic value.
Laccases are multicopper containing enzymes capable of performing one electron oxidation of a broad range of substrates. Using molecular oxygen as the final electron acceptor, t
Laccases are multicopper containing enzymes capable of performing one electron oxidation of a broad range of substrates. Using molecular oxygen as the final electron acceptor, t
Autor:
Noé R Rivera, Juan A. Ayala, Aurelio Hidalgo, José Berenguer, Diana M. Mate, Esther Sanchez-Freire
Publikováno v:
Biotechnology and bioengineering. 117(1)
Prolonged stability is a desired property for the biotechnological application of enzymes since it allows its reutilization, contributing to making biocatalytic processes more economically competitive with respect to chemical synthesis. In this study
Publikováno v:
Chemistry – A European Journal. 26:13533-13533
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Chemistry-a European journal 26(60), 13568-13572 (2020). doi:10.1002/chem.202002740
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Chemistry-a European journal 26(60), 13568-13572 (2020). doi:10.1002/chem.202002740
Staphylococcus aureus sortase A (SaSrtA) is widely used for site‐specific protein modifications, but it lacks the robustness for performing bioconjugation reactions at elevated temperatures or in presence of denaturing agents. Loop engineering and