In order to find the difference between the cleavage sites in bovine milk proteins by metalloproteinase from Paenibacillus spp. BD3526 and chymosin, the peptides generated from αs1-, αs2- and κ-casein and β-lactoglobulin (β-Lg) digested by the enzymes were analyzed by high performance liquid chromatography coupled with quadruple-timeof- flight mass spectrometer (HPLC-Q-TOF-MS-MS). The results indicated that the cleavage sites in bovine milk proteins by metalloproteinase and chymosin shared high similarity and both of these enzymes specifically cleaved the Lys-Thr, Lys-Phe, Arg- Phe and Arg-Tyr peptide bonds to generate peptides with ACE inhibitory, antimicrobial and immunomodulating activities.

Phellinus baumii is a highly-valued medicinal mushroom. In the current study, inhibitory effects of different concentrations of the 95% ethanol extract from Phellinus baumii were examined on Gram-positive, Gram-negative, molds and yeasts. The results showed that the Phellinus baumii ethanol extract at concentrations in the range of 0.1 to 5 mg/mL was effective against the growth of harmful bacteria and fungi and could obviously control the total number of bacteria in milk without having any significant adverse impact on beneficial bacteria. Meanwhile, the extract had a broader antimicrobial spectrum than antimicrobials such as nisin, suggesting its potential application for inhibiting harmful microorganisms in milk and dairy products.