Sökning: AMNE:(NATURAL SCIENCES) AMNE:(Chemical Sciences) AMNE:(Materials Chemistry) >
Improved enzymatic ...
Improved enzymatic activity of Thermomyces lanuginosus lipase immobilized in a hydrophobic particulate
-
- Sörensen, Malin H. (författare)
- YKI, Institute for Surface Chemistry,YKI, Inst Surface Chem, SE-11486 Stockholm, Sweden
-
- Ng, Jovice Boon Sing, 1975- (författare)
- Stockholms universitet,Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi,Materials Chemistry Research Group,Institutionen för material- och miljökemi (MMK)
-
- Bergström, Lennart (författare)
- Stockholms universitet,Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi,Materials Chemistry Research Group,Institutionen för material- och miljökemi (MMK)
-
visa fler...
-
- Alberius, Peter (författare)
- YKI, Institute for Surface Chemistry
-
visa färre...
-
(creator_code:org_t)
- Elsevier Inc. 2010
- 2010
- Engelska.
-
Ingår i: Journal of Colloid and Interface Science. - : Elsevier Inc.. - 0021-9797 .- 1095-7103. ; 343:1, s. 359-365
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
https://urn.kb.se/re...
-
https://urn.kb.se/re...
-
visa färre...
Abstract
Ämnesord
Stäng
- Lipase from Thermomyces lanuginosus has been immobilized within particulate mesoporous silica carriers, with either hydrophilic or hydrophobic supporting surfaces, produced by the newly developed emulsion and solvent evaporation (ESE) method. The Michaelis-Menten model was used to calculate the parameters related to the enzymatic activity of lipase i.e. the turnover number, kcat, and the specific activity. The specific activity was improved by immobilization of lipase onto the hydrophobic support, compared to lipase immobilized onto the hydrophilic support and lipase free in solution. The enhanced enzymatic activity of lipase onto a hydrophobic support was attributed to interfacial activation of the Thermomyces lanuginosus lipase when it is attached to a hydrophobic surface and a reduced denaturation. Confocal scanning laser microscopy (CLSM) studies, of fluorescently tagged lipase, showed that leakage of the lipase from the mesoporous particles was limited to an initial period of only a few hours. Both the rate and the amount of lipase leached were reduced when the lipase was immobilized onto the hydrophobic support.
Ämnesord
- NATURVETENSKAP -- Kemi -- Oorganisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Inorganic Chemistry (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Kemiteknik -- Kemiska processer (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Chemical Engineering -- Chemical Process Engineering (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Materialteknik -- Annan materialteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Materials Engineering -- Other Materials Engineering (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Andra medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Other Basic Medicine (hsv//eng)
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Nyckelord
- Enzyme
- lipase
- mesoporous
- silica
- immobilization
- hydrophobic
- spheres
- particles
- Bio-inorganic chemistry
- Bio-oorganisk kemi
- Bioengineering
- Bioteknik
- Catalysis
- Katalys
- Functional materials
- Funktionella material
- Inorganic Chemistry
- oorganisk kemi
- Chemistry
- fysikalisk kemi
- Surface and colloid chemistry
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas