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Updated: Aug 14, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
[Polarograhic adsorptive wave of protein hydrolysate in Pb2+ and sodium hydroxide solution and its application]
Jin-Gui Lan1, Deng-Bai Luo, Yu-Hua Zhang
1College of Chemistry and Life Science, South Central University for Nationalities, Wuhan 430074, China.
Aim:
To propose a new simple and sensitive voltammetric method for determination of proteins.
Methods:
Protein with sulfhydryl or disulfide bond in 0.5 mol x L(-1) NaOH, 1.5 x 10(-4) mol x L(-1) Pb2+ and 0.02% tetrabutylammonium iodide was heated in boiling water for 5 minutes. The reactive product gave a well defined reductive adsorption wave at -0.66 V (vs SCE) by means of single sweep polarography, and the height of derivative wave was proportional to the concentration of proteins.
Results:
The peak height was linearly proportional to bovine serum albumin (BSA) or human serum albumin (HSA) concentration in range of 7.5 x 10(-10) -3.0 x 10(-7) mol x L(-1) (r(BSA) = 0.9995, and r(HSA) = 0.9990). The detection limit of BSA or HSA was 3.0 x 10(-10) mol x L(-1). For lysozyme (Lyso), the concentration range was from 1.4 x 10(-8) to 1.3 x 10(-6) mol x L(-10 (r(Lyso) = 0.9997) and the detection limit was 7.0 x 10(-9) mol x L(-1).
Conclusion:
The method is simple, rapid, sensitive and applicable to the assay of diluted human serum albumin samples.
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