Zobrazeno 1 - 10
of 150
pro vyhledávání: '"Cross-linked enzyme aggregate"'
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Ziyi Liu, Stephen R. Smith
Publikováno v:
Microorganisms, Vol 11, Iss 8, p 1902 (2023)
Enzymes are used extensively as industrial bio-catalysts in various manufacturing and processing sectors. However, commercial enzymes are expensive in part due to the high cost of the nutrient medium for the biomass culture. Activated sludge (AS) is
Externí odkaz:
https://doaj.org/article/55f11761e4864a88819c82931ddd1639
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
In this study, a strain with rutin degrading enzyme (RDE) activity was screened from moldy tartary buckwheat and subsequently identified as Fusarium spp. The structure and enzyme characteristics of CLEA-RDE formed by immobilization via cross-linking
Externí odkaz:
https://doaj.org/article/618227d8f86f4a70a7ae11f53e9689ae
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
Environmental Science and Pollution Research. 28:44051-44063
Despite all its advantages and potential, cross-linking enzyme aggregate (CLEA) technology is still not applied at an industrial scale for enzyme insolubilization for bioremediation purposes. In this study, the enzyme polymer engineered structure (EP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd3b041269cd487c126737f6d8ae8440
https://doi.org/10.1007/s11356-021-13746-4
https://doi.org/10.1007/s11356-021-13746-4
Publikováno v:
Applied Microbiology and Biotechnology. 105:1925-1941
Background: A novel Aspergillus. niger strain GZUF36 with two high sn-1,3 position selectivity of lipases, including an intracellular lipase and an extracellular one was selected from oil-rich soil in our previous work. The sn-1,3 extracellular lipas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2fc2fc85f11e598ec368c757190b3b7
https://doi.org/10.1007/s00253-021-11160-x
https://doi.org/10.1007/s00253-021-11160-x
Publikováno v:
International Journal of Biological Macromolecules. 169:541-550
Genipin is a nontoxic natural cross-linker that was successfully used to prepare cross-linked enzyme aggregates (CLEAs) of Trametes versicolor laccase. The recovered activity of CLEAs was influenced by the co-solvent type, genipin concentration, cros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c5b0112bd4531a90cb8e8926873f6c1
https://doi.org/10.1016/j.ijbiomac.2020.12.136
https://doi.org/10.1016/j.ijbiomac.2020.12.136
Autor:
Murugan Marudhamuthu, Suganya Kannan
Publikováno v:
International Journal of Biological Macromolecules. 141:218-231
In this study, L-methioninase (METs) was precipitated from Pseudomonas putida MTCC 9782 and was cross-linked with a cross-linking agent glutaraldehyde to obtain a catalytically active insoluble enzyme. Among the various precipitants tested, ammonium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f85ee13029977de7f6f8281de90d0b4d
https://doi.org/10.1016/j.ijbiomac.2019.08.246
https://doi.org/10.1016/j.ijbiomac.2019.08.246
Autor:
Hesham A. El-Enshasy, Jamaliah Md Jahim, Abdul Munir Abdul Murad, Mohd Khairul Hakimi bin Abdul Wahab, Farah Diba Abu Bakar, Rosli Md. Illias
Publikováno v:
Process Biochemistry. 86:40-49
Cross-linked enzyme aggregate (CLEA) is a well-known enzyme immobilization technique that is efficient and cost-effective. In this study, we proposed a combination of the surface modification of an enzyme and CLEA to increase the number of free amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dac5831cff7fb49d5ee0134282082530
https://doi.org/10.1016/j.procbio.2019.07.017
https://doi.org/10.1016/j.procbio.2019.07.017