In-vitro antioxidant and antibacterial properties of fermentatively and enzymatically prepared chicken liver protein hydrolysates.

Protein hydrolysates were prepared from chicken liver using fermentation and enzymatic hydrolysis. The lactic acid bacteria Pediococcus acidilactici NCIM5368 was employed in the fermentation process and a commercial protease (Alcalase® 2.5) was used in enzymatic hydrolysis. Chicken liver hydrolysates prepared by fermentation (FCLH) and enzymatic hydrolysis (ECLH) revealed appreciable amounts of protein [55.85 and 61.34 %; on dry weight basis, respectively]. Fermentation and enzymatic hydrolysis resulted in 14.3 and 26.12 % of degree of hydrolysis. Total antioxidant activity, reducing power, scavenging of superoxide, 2- diphenyl-1-picrylhydrazyl (DPPH) and 2, 2-azino-bis-3-ethyl-benzthiazoline-6-sulphonic acid (ABTS) radicals were determined for both FCLH & ECLH. FCLH & ECLH showed total antioxidant activity of 0.99 and 1.13 µg AAE mg(-1) proteins, respectively; while, they scavenged 96.14 and 92.76 % of DPPH radicals respectively. FCLH showed higher ABTS radical scavenging activity (32.16 %) than ECLH (19.29 %). Superoxide anion scavenging activity of FCLH & ECLH were found to be 95.02 & 88.94 %, respectively. Residues obtained after both treatments also exhibited antioxidant activities. FCLH reported highest antagonistic activity against Listeria monocytogenes (30 mm); while, ECLH showed antibacterial activity only against Micrococcus luteus (12 mm). Both hydrolysates have the potential to be a protein rich ingredient for use in formulated foods and possible help in reduction of oxidative stress.

Structural and antimicrobial properties of Maillard reaction products in chicken liver protein hydrolysate after sonication.

This study aimed to investigate the structural and antimicrobial properties of Maillard reaction products (MRPs) in chicken liver protein (CLP) and its hydrolysate (CLPH) after sonication (SCLPH). The MRPs of CLP (CLPM), CLPH (CLPHM) and SCLPH (SCLPHM) were analyzed by several spectrometric techniques. The molecular weights of the CLPHM and SCLPHM were primarily between 1.35 kDa and 17 kDa. Moreover, the molecular weights in the CLPHM and SCLPHM below 1.35 kDa were increased, which indicated that cross-linking and thermal degradation occurred during the Maillard reaction (MR). The SCLPHM showed an obvious network skeleton, and the surface had many small crystal-shaped particles after ultrasound treatment and MR by scanning electron microscopy. The SCLPHM had more negative charges than the CLPHM, thus effectively inhibiting the growth of S. saprophyticus and E. coli. MR and ultrasound treatment could be a promising technology to expand the application prospects of low-value meat byproducts.