The mutton flavor is affected by cooking water significantly, and the flavor of mutton is delicious and widely loved by consumers through an extremely simple processing in northwest China, such as Inner Mongolia, Ningxia, and Xinjiang. The flavor shows obvious changes if get out of these areas even use the same raw meat, which may be caused by different cooking water. To determine whether and how the cooking water affect the mutton soup flavor, the elements in water, the flavor was studied by inductively coupled plasma mass spectrometry (ICP‐MS), amino acid analyzer, and thermal desorption (TDS)–gas chromatography–mass spectrometry (GC‐MS). Specifically, three water samples from different sources, Ningxia (NXW), Beijing (BJW), and ultrapure water from the laboratory (PUW), were used for cooking with Tan sheep's ribs to get different mutton soups. The inductively coupled plasma mass spectrometry (ICP‐MS) results showed that the elements and the concentration of solutes in different water sources were significantly different. The NXW batch had the highest Na, Mg, K, and Sr concentrations, and Na in NXW water reached to 50.60 mg/L, which existed as Na⁺, significantly (p < .05) higher than BJW (8.63 mg/L) and PUW, which were important to the flavor of mutton soup. The PUW batch had the highest content of free amino acids, and the content of glutamic acid (Glu) reached to 17.89 μg/mL. The NXW batch had the highest content of taste nucleotides, and the content of 5´‐IMP reached to 68.68 μg/ml. The volatiles of the three batches had significant differences, and only 40 volatiles were detected in all batches. Further flavor studies using electronic nose and electronic tongue showed significant differences in overall aroma and overall taste, especially bitterness, saltiness, and astringency. The results could provide a basis for improving the flavor quality for the mutton soup.

The growth of bacteria and fungi may cause disease inf human or spoilage of food. New antimicrobial substances need to be discovered. Lactoferricin (LFcin) is a group of antimicrobial peptides derived from the N-terminal region of the milk protein lactoferrin (LF). LFcin has antimicrobial ability against a variety of microorganisms, which is significantly better than that of its parent version. Here, we review the sequences, structures, and antimicrobial activities of this family and elucidated the motifs of structural and functional significance, as well as its application in food. Using sequence and structural similarity searches, we identified 43 new LFcins from the mammalian LFs deposited in the protein databases, which are grouped into six families according to their origins (Primates, Rodentia, Artiodactyla, Perissodactyla, Pholidota, and Carnivora). This work expands the LFcin family and will facilitate further characterization of novel peptides with antimicrobial potential. Considering the antimicrobial effect of LFcin on foodborne pathogens, we describe the application of these peptides from the prospective of food preservation.