|
|
||||||||
Department of Food Technology, Iowa State University, Ames 50011
ABSTRACT
Propionibacterium shermanii P59 produced free proline in large amounts from peptide-containing media. Enzymatic casein hydrolysates were better substrates than meat hydrolysates. Some proline was produced by proteolysis of casein, but the production rate was slower than by peptidase action on casein hydrolysates. Proline biosynthesis from arginine probably was more important than from glutamic acid, and biosynthesis was probably less significant than peptide hydrolysis in producing free proline. Intracellular proline was small compared with free proline produced in the media. Release of proline from peptides coincided with the release of cell proteins and enzymes into the medium.
1 Journal Paper No. J-8497 of the Iowa Agriculture and Home Economics Experiment Station, Ames 50011. Project No. 1839.
2 The Dairy Research Institute, Box 36, The Agricultural University of Norway, N-1432 Vollebekk, Norway.
3 Vice President-Research and Development, Leprino Cheese Company, P.O. Box 8400, Denver, CO 80201.
This article has been cited by other articles:
![]() |
J. Treimo, G. Vegarud, T. Langsrud, and K. Rudi Use of DNA Quantification To Measure Growth and Autolysis of Lactococcus and Propionibacterium spp. in Mixed Populations Appl. Envir. Microbiol., September 1, 2006; 72(9): 6174 - 6182. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Leenhouts, A. Bolhuis, J. Boot, I. Deutz, M. Toonen, G. Venema, J. Kok, and A. Ledeboer Cloning, Expression, and Chromosomal Stabilization of the Propionibacterium shermanii Proline Iminopeptidase Gene (pip) for Food-Grade Application in Lactococcus lactis Appl. Envir. Microbiol., December 1, 1998; 64(12): 4736 - 4742. [Abstract] [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |