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Removal of Copper in Microdroplets by Ovomucoid Hydrolysates Bound to Reverse-Phase Chromatography Media Within

Youji Shimazaki1,2, Suzuka Inoue3

  • 1Department of Chemistry and Biology, Graduate School of Science and Engineering (Science Section), Ehime University, Matsuyama City, 790-8577, Japan. shimazaki.yoji.my@ehime-u.ac.jp.

Applied Biochemistry and Biotechnology
|May 19, 2019
PubMed

Insights

Hydrolyzed ovomucoid (OVM) effectively removes copper ions (Cu2+) from microdroplets using chromatography media. This novel method utilizes digested OVM bound to pipette tip columns for efficient metal ion chelation.

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Materials Science

Background:

  • Ovomucoid (OVM) is a glycoprotein in egg white.
  • Proteolytic hydrolysis can alter OVM's properties.
  • Copper ions (Cu2+) are relevant in biological and environmental samples.

Purpose of the Study:

  • To investigate the Cu2+-chelating activity of OVM hydrolysates.
  • To develop a method for removing Cu2+ from microdroplets using OVM.
  • To assess the efficiency of OVM hydrolysates bound to chromatography media for Cu2+ removal.

Main Methods:

  • Ovomucoid (OVM) was hydrolyzed using subtilisin A.
  • OVM hydrolysates were bound to C4 and C18 reverse-phase chromatography media in pipette tips.
  • Cu2+ removal efficiency was quantified in microdroplets.
  • Non-denaturing electrophoresis and Cu2+ staining were used to analyze OVM polypeptides.

Main Results:

  • OVM hydrolysates exhibited significant Cu2+-chelating activity.
  • Digested OVM bound to C4 and C18 media removed 2.1 and 2.4 nmol of Cu2+, respectively.
  • Non-digested OVM showed lower Cu2+ removal (0.6 and 1.0 nmol).
  • Increased OVM digestion correlated with higher Cu2+ removal.

Conclusions:

  • OVM hydrolysates bound to chromatography media in pipette tips offer an effective method for Cu2+ removal from microdroplets.
  • This approach has potential applications in sample preparation and analysis of biological samples.
  • The study highlights the utility of enzyme-modified proteins for metal ion chelation.
Keywords:
Copper removalElectrophoresisReverse-phase chromatography mediaSubtilisin AZipTip

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