Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Dong-Hao Zhang"'
Publikováno v:
Materials & Design, Vol 220, Iss , Pp 110865- (2022)
To firmly immobilize enzyme on carrier surface without covalent attachment as well as improve enzyme stability, an effective method of enzyme immobilization was developed by encapsulating enzyme into nano-molecular cages on the surface of magnetic mi
Externí odkaz:
https://doaj.org/article/fb07fb94e6324ff6b6c6c92321fd6f9e
Publikováno v:
Journal of Chemistry, Vol 2013 (2013)
Enzyme immobilization has been investigated to improve lipase properties over the past few decades. Different methods and various carriers have been employed to immobilize enzyme. However, the application of enzymatic technology in large scale is rar
Externí odkaz:
https://doaj.org/article/ef90d2afaf7c422eb18948ddd60e1cc1
Publikováno v:
Small. :2301413
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b251cf5f52c2e6ea8ce2b81211f669c
https://doi.org/10.1002/smll.202301413
https://doi.org/10.1002/smll.202301413
Publikováno v:
Food Chemistry. 364:130428
To improve the performance of lipase in biosynthesis of benzyl cinnamate, a new immobilized lipase by entrapping enzyme into nano-molecular cages was designed. Consequently, the entrapped lipase showed a robust immobilization, which diminished the le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3672a44f5e6ce05b97c9a0572d8626ed
https://doi.org/10.1016/j.foodchem.2021.130428
https://doi.org/10.1016/j.foodchem.2021.130428
Publikováno v:
Journal of Chemical Technology & Biotechnology. 93:994-1002
BACKGROUND Polyethyleneimine (PEI) had attracted wide interest due to not only its good hydrophilicity but also its high density of amino groups across the polymer chain. In order to study deeply the effect of PEI as spacer arm on dye ligand modifica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::662adafa31cb28fe6548e4b2c6772ff9
https://doi.org/10.1002/jctb.5451
https://doi.org/10.1002/jctb.5451
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 133:136-143
In order to obtain a deep insight into the effects of spacer arms on performing CB modification and dye-affinity adsorption, poly(methyl methacrylate) (PMMA) magnetic microspheres were prepared and modified respectively with poly(ethylene glycol) (PE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::20a8f7967d38dc1df9fcb294aa1bf167
https://doi.org/10.1016/j.molcatb.2016.08.007
https://doi.org/10.1016/j.molcatb.2016.08.007
Publikováno v:
Food Chemistry. 190:629-633
In this paper, Lipozyme TLIM-catalyzed synthesis of ethyl cinnamate through esterification of cinnamic acid with ethanol was studied. In order to increase the yield of ethyl cinnamate, several media, including acetone, isooctane, DMSO and solvent-fre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a3df9fe554540babccb8a09e2560b4f
https://doi.org/10.1016/j.foodchem.2015.06.017
https://doi.org/10.1016/j.foodchem.2015.06.017
Publikováno v:
Bioresource Technology. 198:256-261
In this study, lipase catalysis was successfully applied in synthesis of benzyl cinnamate through esterification of cinnamic acid with benzyl alcohol. Lipozyme TLIM was found to be more efficient for catalyzing this reaction than Novozym 435. In orde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc08e11640e46ce640e7a4c48fa1646f
https://doi.org/10.1016/j.biortech.2015.09.028
https://doi.org/10.1016/j.biortech.2015.09.028
Publikováno v:
Colloids and Surfaces B: Biointerfaces. 129:206-210
Poly(vinyl acetate-acrylamide) microspheres with an average diameter of 2-4μm were successfully prepared and characterized via SEM and FTIR. Then the microspheres were modified with epoxy groups through reacting with epichlorohydrin and used as carr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83b717fe7848750357468ecf9c4c0c21
https://doi.org/10.1016/j.colsurfb.2015.03.056
https://doi.org/10.1016/j.colsurfb.2015.03.056