Details
| Original language | English |
|---|---|
| Pages (from-to) | 2344-2353 |
| Number of pages | 10 |
| Journal | Journal of Agricultural and Food Chemistry |
| Volume | 66 |
| Issue number | 10 |
| Early online date | 10 Aug 2016 |
| Publication status | Published - 14 Mar 2018 |
Abstract
Some l-arginyl dipeptides were recently identified as salt taste enhancers, thus opening the possibility to reduce dietary sodium uptake without compromising palatability. A screening of 15 basidiomycete fungi resulted in the identification of 5 species secreting a high peptidolytic activity (>3 kAU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that l-arginyl dipeptides were liberated when casein or lysozyme served as substrate. Much higher yields of dipeptides (42-75 μmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest l-arginyl dipeptide yields and a significant salt taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and nonspecific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.
Keywords
- basidiomycota, casein, L-arginyl dipeptides, lysozyme hydrolysis, salt taste enhancers
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Agricultural and Biological Sciences(all)
- General Agricultural and Biological Sciences
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In: Journal of Agricultural and Food Chemistry, Vol. 66, No. 10, 14.03.2018, p. 2344-2353.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Salt Taste Enhancing l -Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota
AU - Harth, Lisa
AU - Krah, Ulrike
AU - Linke, Diana
AU - Dunkel, Andreas
AU - Hofmann, Thomas
AU - Berger, Ralf G.
N1 - Funding information: This project (AIF 16721 N) was supported by the Arbeitsgemeinschaft industrieller Forschungsvereinigungen “Otto von Guericke” e. V. (AiF) through FEI (Forschungskreis der Ernahrungsindustrië e. V., Bonn). Notes The authors declare no competing financial interest.
PY - 2018/3/14
Y1 - 2018/3/14
N2 - Some l-arginyl dipeptides were recently identified as salt taste enhancers, thus opening the possibility to reduce dietary sodium uptake without compromising palatability. A screening of 15 basidiomycete fungi resulted in the identification of 5 species secreting a high peptidolytic activity (>3 kAU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that l-arginyl dipeptides were liberated when casein or lysozyme served as substrate. Much higher yields of dipeptides (42-75 μmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest l-arginyl dipeptide yields and a significant salt taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and nonspecific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.
AB - Some l-arginyl dipeptides were recently identified as salt taste enhancers, thus opening the possibility to reduce dietary sodium uptake without compromising palatability. A screening of 15 basidiomycete fungi resulted in the identification of 5 species secreting a high peptidolytic activity (>3 kAU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that l-arginyl dipeptides were liberated when casein or lysozyme served as substrate. Much higher yields of dipeptides (42-75 μmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest l-arginyl dipeptide yields and a significant salt taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and nonspecific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.
KW - basidiomycota
KW - casein
KW - L-arginyl dipeptides
KW - lysozyme hydrolysis
KW - salt taste enhancers
UR - http://www.scopus.com/inward/record.url?scp=85043781723&partnerID=8YFLogxK
U2 - 10.1021/acs.jafc.6b02716
DO - 10.1021/acs.jafc.6b02716
M3 - Article
C2 - 27509299
AN - SCOPUS:85043781723
VL - 66
SP - 2344
EP - 2353
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 10
ER -