HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Eitenmiller, R. R. Articles by Shahani, K. M. Search for Related Content PubMed PubMed Citation Articles by Eitenmiller, R. R. Articles by Shahani, K. M.

Relationship Between Composition and Stability of Bovine Milk Lysozyme¹

Department of Food Science and Technology, University of Nebraska, Lincoln 68503

ABSTRACT

The amino acid analysis, peptide mapping, and heat stability of bovine milk lysozyme are presented. The bovine milk lysozyme molecule contains approximately 154 amino acids and is strikingly different in amino acid content from human milk lysozyme and egg white lysozyme. Tryptic hydrolysis yielded 26 peptides, all of which are unique from tryptic peptides of human milk lysozyme and egg white lysozyme. In addition, bovine milk lysozyme was more heat stable than human milk lysozyme at pH 4.0 but more labile at pH 7.0 and 9.0. Possible explanations for the differences in heat stability are discussed

¹ Published as paper No. 3852, Journal Series, Agricultural Experiment Station, Lincoln, NE. Research was conducted on project 16-17. This work was supported in part by a US Public Health research grant HD-00858 from the National Institute of Child Health and Human Development.

² Department of Food Science, University of Georgia, Athens, GA 30602.

³ 3707 Tangelwood Drive, Bryan, TX 77801.