Milk protein is a well-known precursor protein for the generation of bioactive peptides using lactic acid bacteria. This study investigated the antioxidant activity of bovine casein hydrolysate after fermentation with Bifidobacterium longum KACC91563 using the 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) assay and total phenolic content (TPC). The antioxidant activities of the 24-h and 48-h hydrolysates were higher than that of the 4-h hydrolysate (2,045.5 and 1,629.3 μM gallic acid equivalents, respectively, vs. 40.3 μM) in the ABTS assay. In contrast, TPC values showed activities of 43.2 and 52.4 μM gallic acid equivalents for the 4-h and 24-h hydrolysates, respectively. Three fractions (≥10 kDa, ≥3 but <10 kDa, and <3 kDa) were separated from the 24-h hydrolysate by ultrafiltration. Among these fractions, the <3 kDa fraction exhibited the highest antioxidant activity (936.7 μM) compared with the other fractions (42.1 and 34.2 μM for >10 kDa and 3-10 kDa fractions, respectively). Through liquid chromatography-electrospray ionization-tandem mass spectrometry analysis, 2 peptides, VLSLSQSKVLPVPQK and VLSLSQSKVLPVPQKAVPYPQRDMPIQA, containing the fragment VLPVPQ that has antioxidant properties, were identified in the <3kDa fraction after 24h of hydrolysis. The present study demonstrates the possibility of antioxidant peptide production from bovine casein using Bifidobacterium longum.
The techno-functional properties of ovomucin as a gel-forming agent and its biological properties are well-known. The aim of the present study was to investigate antioxidant activity in ovomucin hydrolysate using radical scavenging assays. Electrophoresis showed that ovomucin isolated from whole egg was well separated. Ovomucin hydrolysis was carried out using microbial protease according to different incubation times. These ovomucin hydrolysates exhibited 85% antioxidant activity as measured by the 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) assay after a 2 h incubation with protease and retained 90% activity until 24 h. At an incubation time of 4 h, the activity of ovomucin hydrolysates reached approximately 90%, corresponding to 115 μM gallic acid equivalent, regardless of the proteases used. The partially purified fraction of the hydrolysate by ultrafiltration and reverse-phase high-performance liquid chromatography was collected and then analyzed by liquid chromatography electrospray ionization mass spectrometry. Two peptides, LDEPDPL and NIQTDDFRT, in this fraction were identified. The antioxidant activities of these two synthesized peptides were measured to be 51.8 and 24.7% by the 2,2-diphenyl-1-picrylhydrazyl assay.
Norovirus infections were detected in 114 of 762 children with acute gastroenteritis in South Korea from November 2005 to November 2006. Seasonality peaks in December, March, and October were also assessed in this study. We identified seven noroviral genotypes (GI-6, GII-2, GII-3, GII-4, GII-5, GII-6, and GII-8) and a C1-120 strain showing low identity (79.3%) with GII-13 and GII-17.
Here, we report gold
nanoparticle-coated starch magnetic beads (AuNP@SMBs) that were prepared
by in situ synthesis of AuNPs on the surface of SMBs. Upon functionalization
of the surface with a specific antibody, the immuno-AuNP@SMBs were
found to be effective in separating and concentrating the target pathogenic
bacteria, Escherichia coli O157:H7,
from an aqueous sample as well as providing a hotspot for surface-enhanced
Raman scattering (SERS)-based detection. We employed a bifunctional
linker protein, 4× gold-binding peptide-tagged Streptococcal
protein G (4GS), to immobilize antibodies on AuNP@SMBs and AuNPs in
an oriented form. The linker protein also served as a Raman reporter,
exhibiting a strong and unique fingerprint signal during the SERS
measurement. The amplitude of the SERS signal was shown to have a
good correlation with the concentration of target bacteria ranging
from 100 to 105 CFU/mL. The detection limit
was determined to be as low as a single cell, and the background signals
derived from nontarget bacteria were negligible due to the excellent
specificity and colloidal stability of the immuno-AuNP@SMBs and SERS
tags. The highly sensitive nature of the SERS-based detection system
will provide a promising means to detect the pathogenic microorganisms
in food or clinical specimen.
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