In vitro evaluation of feed-grade enzyme activity at pH levels simulating various parts of the avian digestive tract

T. Ao, A. H. Cantor, A. J. Pescatore, J. L. Pierce

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

The activities of β-glucanase, xylanase, amylase, α-galactosidase and protease were measured at their published optimum pH levels and at pH levels of 3.0, 6.0, 6.5, 7.0 and 7.5 to simulate pH levels of the gizzard, the diet, the crop, and the proximal and distal parts of small intestine, respectively. The activity of β-glucanase was determined by measuring reducing sugars after incubation of β-glucan. Xylanase activity was assayed by measuring xylose after hydrolysis of xylan. The activity of amylase was measured through hydrolysis of soluble starch. The assay of α-galactosidase was based on a hydrolysis of p-nitrophenyl-α-d-galactoside followed by measurement of liberated p-nitrophenol. The activity of protease was assayed by measuring tyrosine after enzymatic hydrolysis of casein. β-Glucanase had high activity at pH levels of 3.0-7.0. Xylanase had no enzyme activity at pH 3.0, but had high activity at pH levels of 6.0-7.0. Amylase had high activity at pH levels of 6.0 and 6.5 but had no or very low activity at pH 3.0, 7.0 and 7.5. α-Galactosidase had high activity at pH 6, but not at other pH levels tested. Protease had either no or very low activity at all pH levels except at pH 3.0. These results suggest that the pH levels commonly found in the avian digestive tract may be a limiting factor for maximum activity of the exogenous enzymes, such as amylase, α-galactosidase and protease.

Original languageEnglish
Pages (from-to)462-468
Number of pages7
JournalAnimal Feed Science and Technology
Volume140
Issue number3-4
DOIs
StatePublished - Jan 15 2008

Keywords

  • Amylase
  • Enzyme activity
  • In vitro assay
  • Protease
  • pH
  • α-Galactosidase

ASJC Scopus subject areas

  • Animal Science and Zoology

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