Facile enzyme immobilization and assay technique using polyethyleneimine-cellulose thin-layer chromatography as a solid support

Jae Chul Pyun, Ann Soo Jang, Jong Sang Park

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

In the search for a plate-shaped solid support for enzyme immobilization, we found commercially obtainable polyethyleneimine (PEI)-cellulose thin-layer chromatography (TLC) plates to have adequate physical and chemical properties for enzyme immobilization. Through Benedict's, Tollens' and ninhydrin tests, the PEI-cellulose coating proved to have enough physical strength and amine concentration, and its properties could be maintained nearly constantly during the processes of enzyme immobilization. To confirm that the PEI-cellulose TLC plate was a suitable support for enzyme immobilization, alkaline phosphatase was immobilized using glutaraldehyde as a crosslinking reagent. The activity of the immobilized alkaline phosphatase was assayed with a reiterative method using p-nitrophenyl phosphate as a substrate. By analyzing Lineweaver-Burk plots from the results of successive assays, we proved the immobilized alkaline phosphatase to be reusable many times.

Original languageEnglish
Pages (from-to)41-44
Number of pages4
JournalEnzyme and Microbial Technology
Volume18
Issue number1
DOIs
Publication statusPublished - 1996 Jan 1

Fingerprint

Enzyme immobilization
Thin layer chromatography
Enzyme Assays
Thin Layer Chromatography
Immobilization
Assays
Cellulose
Phosphatases
Alkaline Phosphatase
Enzymes
Cross-Linking Reagents
Ninhydrin
Glutaral
Crosslinking
Chemical properties
Amines
Phosphates
Physical properties
Coatings
polyethyleneimine-cellulose

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

Cite this

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Facile enzyme immobilization and assay technique using polyethyleneimine-cellulose thin-layer chromatography as a solid support. / Pyun, Jae Chul; Jang, Ann Soo; Park, Jong Sang.

In: Enzyme and Microbial Technology, Vol. 18, No. 1, 01.01.1996, p. 41-44.

Research output: Contribution to journalArticle

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