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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
Published on: April 4, 2014
Identification and characterization of flavor precursor peptide from beef enzymatic hydrolysate by Maillard reaction
Le Kang1, Aygul Alim1, Huanlu Song1
1Beijing Advanced Innovation Center for Food Nutrition and Human Health, Laboratory of Molecular Sensory Science, Beijing Technology and Business University, Beijing 100048, China.
Abstract:
In this study, beef enzymatic hydrolysate was fractionated by sequential UF/GFC/RP-HPLC. RP-HPLC fractions were subjected to Maillard reaction with xylose. The FD/TD factors of the MRPs were prominent. Sensory evaluation showed that F-3 exhibited intense meaty taste; the kokumi intensity, umami-enhancing capacity in F-4; the umami-enhancing capacity in F-5; the umami intensity and umami-enhancing capacity in F-6. All these were strong in F-7 and F-8. The RP-HPLC fractions were subsequently analyzed by ESI-Q-TOF MS/MS. Of the 21 peptides identified, Leu(Ile)-X, Val-X, Phe-X, and Cys-containing peptides were the major ones. Six peptides (Leu-Cys, Glu-Cys-Gly, Cys-Gly-Val, Val-Met, Phe-Glu, and Phe-Gln) were synthesized and included in the Maillard reaction with xylose. FD factors of MRPs of all these synthesized peptides were significantly greater than those of fraction F-7. The stronger Maillard reactivity demonstrated by the synthesized peptides proves that this work is correct.
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