Surface Chemistry Studies on the Formation of Mixed Stearic Acid/Phenylalanine Dehydrogenase Langmuir and Langmuir-Blodgett Films

This work investigates the physicochemical properties of mixed stearic acid (HSt)/phenylalanine dehydrogenase enzyme (PheDH) Langmuir films and their immobilization onto solid supports as Langmuir-Blodgett (LB) films. PheDH from the aqueous subphase enters the surfactant matrix up to an exclusion su...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1999. - 37(2021), 25 vom: 29. Juni, Seite 7771-7779
1. Verfasser: da Silva, Rafael Leonardo Cruz Gomes (VerfasserIn)
Weitere Verfasser: Sharma, Shiv K, Paudyal, Suraj, Mintz, Keenan J, Leblanc, Roger M, Caseli, Luciano
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Stearic Acids stearic acid 4ELV7Z65AP Amino Acid Oxidoreductases EC 1.4.- phenylalanine oxidase EC 1.4.3.-
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245 1 0 |a Surface Chemistry Studies on the Formation of Mixed Stearic Acid/Phenylalanine Dehydrogenase Langmuir and Langmuir-Blodgett Films 
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520 |a This work investigates the physicochemical properties of mixed stearic acid (HSt)/phenylalanine dehydrogenase enzyme (PheDH) Langmuir films and their immobilization onto solid supports as Langmuir-Blodgett (LB) films. PheDH from the aqueous subphase enters the surfactant matrix up to an exclusion surface pressure of 25.3 mN/m, leading to the formation of stable and highly condensed mixed Langmuir monolayers. Hydrophobic interactions between the enzyme and HSt nonpolar groups tuned the secondary structure of PheDH, evidenced by the presence of β-sheet structures as demonstrated by infrared and circular dichroism spectra. The floating monolayers were successfully transferred to solid quartz supports, yielding Y-type LB films, and then characterized employing fluorescence, circular dichroism, and microscopic techniques, which indicated that PheDH was co-immobilized with HSt proportionally to the number of transferred layers. The enzyme fluidized the HSt monolayers, reducing their maximum dipoles when condensed to their maximum, and disorganized the alkyl chains of the fatty acid, as detected with infrared spectroscopy. The stability of the mixed floating monolayers enabled their transfer to solid supports as LB films, which is important for producing optical and electrochemical sensors for phenylalanine whose molecular architecture can be controlled with precision 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a 4ELV7Z65AP  |2 NLM 
650 7 |a Amino Acid Oxidoreductases  |2 NLM 
650 7 |a EC 1.4.-  |2 NLM 
650 7 |a phenylalanine oxidase  |2 NLM 
650 7 |a EC 1.4.3.-  |2 NLM 
700 1 |a Sharma, Shiv K  |e verfasserin  |4 aut 
700 1 |a Paudyal, Suraj  |e verfasserin  |4 aut 
700 1 |a Mintz, Keenan J  |e verfasserin  |4 aut 
700 1 |a Leblanc, Roger M  |e verfasserin  |4 aut 
700 1 |a Caseli, Luciano  |e verfasserin  |4 aut 
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