Variation in caseinolytic properties of six cheese related Lactobacillus helveticus strains
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Variation in caseinolytic properties of six cheese related Lactobacillus helveticus strains. / Jensen, Marie Elisabeth Penderup; Vogensen, Finn Kvist; Ardö, Ylva Margareta.
In: International Dairy Journal, Vol. 19, No. 11, 2009, p. 661-668.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Variation in caseinolytic properties of six cheese related Lactobacillus helveticus strains
AU - Jensen, Marie Elisabeth Penderup
AU - Vogensen, Finn Kvist
AU - Ardö, Ylva Margareta
PY - 2009
Y1 - 2009
N2 - A large degree of strain variation was observed in caseinolytic properties of six cheese related Lactobacillus helveticus strains. Activity on intact s1- and ß-casein was observed only after growth in milk andnot in MRS. Totally 27 peptides from s1- and 22 from ß-casein were identified from MS/MS fragmentationpatterns. All six strains released peptides from the amino end of s1-casein, and the bonds Ile6-Lys7 and Gln9-Gly10 were identified as primary cleavage sites. Strain variation in the activity on intact ß-casein was observed and five of the six strains released peptides from the C-terminal region. The strains had very different activities and some strains had only trace activities. L. helveticus CNRZ 32 had the highest activity towards s1-casein while L. helveticus LHC2 had the highest activity towards ß-casein, and these two strains also produced unique peptides from both s1- and ß-casein.
AB - A large degree of strain variation was observed in caseinolytic properties of six cheese related Lactobacillus helveticus strains. Activity on intact s1- and ß-casein was observed only after growth in milk andnot in MRS. Totally 27 peptides from s1- and 22 from ß-casein were identified from MS/MS fragmentationpatterns. All six strains released peptides from the amino end of s1-casein, and the bonds Ile6-Lys7 and Gln9-Gly10 were identified as primary cleavage sites. Strain variation in the activity on intact ß-casein was observed and five of the six strains released peptides from the C-terminal region. The strains had very different activities and some strains had only trace activities. L. helveticus CNRZ 32 had the highest activity towards s1-casein while L. helveticus LHC2 had the highest activity towards ß-casein, and these two strains also produced unique peptides from both s1- and ß-casein.
U2 - 10.1016/j.idairyj.2009.04.001
DO - 10.1016/j.idairyj.2009.04.001
M3 - Journal article
VL - 19
SP - 661
EP - 668
JO - International Dairy Journal
JF - International Dairy Journal
SN - 0958-6946
IS - 11
ER -
ID: 15889007