Protein precipitation assay for quantitation of tannins: Determination of protein in tannin-protein complex

Harinder Paul S. Makkar, Rajinder K. Dawra, Bhupinder Singh

Research output: Contribution to journalArticle

75 Scopus citations

Abstract

A protein precipitation method for the determination of tannins has been developed. The protein in the tannin-protein complexes was measured using the ninhydrin assay of amino acids released by alkaline hydrolysis of the complex. Standard protein and the complex were hydrolyzed with 13.5 n NaOH at 120°C for 20 min and the amino acids released were measured with ninhydrin. Tannins did not interfere in the determination of protein by ninhydrin assay. The bovine serum albumin (BSA) precipitated (y;mg) increased linearly with increase in tannic acid (x) from 0.2 to 0.9 mg (y = 2.598x - 0.258). The protein precipitation capacities (mg BSA precipitated/g dry wt) measured by the method for young and mature leaves of oaks were Quercus incana (young, 42.21; mature, 79.51), Q. ilex (young, 1.86; mature, 1.86), and Q. semecarpifolia (young, 733.54; mature, 304.32). The method can provide valuable information on the mechanisms of protein-tannin interactions and nutritional and physiological significances of tannins.

Original languageEnglish (US)
Pages (from-to)435-439
Number of pages5
JournalAnalytical Biochemistry
Volume166
Issue number2
DOIs
StatePublished - Nov 1 1987
Externally publishedYes

Keywords

  • ninhydrin
  • protein-tannin complex
  • tannin determination

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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