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Title: Investigation of enzyme reaction by surface plasmon resonance (SPR) technique
Authors: Thidarat Wangkam
Toemsak Srikhirin
Phenphichar Wanachantararak
Vipul Baxi
Boonsong Sutapun
Rathasart Amarit
Mahidol University
Chiang Mai University
Thailand National Science and Technology Development Agency
Keywords: Engineering;Materials Science;Physics and Astronomy
Issue Date: 4-Jun-2009
Citation: Sensors and Actuators, B: Chemical. Vol.139, No.2 (2009), 274-279
Abstract: An investigation into the surface plasmon resonance (SPR) sensor surface for the detection of enzyme reaction is reported. The thin polymeric film is prepared by spin casting poly (styrene-co-maleic acid) [PSMA] on a chromium/gold-coated SPR substrate. Bovine serum albumin (BSA) is adsorbed onto this surface with a mix of side-on and end-on orientation. The adsorbed BSA was tested against the protease where the cleavage reaction was followed by the change in the resonance angle of the SPR. The kinetic of the enzyme reaction follows the Michaelis-Menten equation where the reaction depends on the concentration of protease. The protease concentration is in the range of 2.5 μg/ml to 1.25 mg/ml. The different topology of protein surface before and after enzyme cleavage was observed by atomic force microscope (AFM). The AFM result shows uncleaved BSA on the surface even at highest protease concentrations owing to the steric hindrance of the adsorbed protease on the BSA surface. The sensor surface can be cleaned by cleaning solution and the surface can be reused, which avoids repetition of the complicated preparing of the sensor surface. © 2009 Elsevier B.V. All rights reserved.
ISSN: 09254005
Appears in Collections:Scopus 2006-2010

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