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 -