B longum KACC 91563 induces apoptosis of mast cells specifically and alleviates food allergy symptoms. Accordingly, B longum KACC 91563 and family 5 extracellular solute-binding protein exhibit potential as therapeutic approaches for food allergies.

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 recent surge in environmental awareness and consumer demand for stable, healthy, and safe foods has led the packaging and food sectors to focus on developing edible packaging materials to reduce waste. Edible films and coatings as a modern sustainable packaging solution offer significant potential to serve as a functional barrier between the food and environment ensuring food safety and quality. Whey protein is one of the most promising edible biopolymers in the food packaging industry that has recently gained much attention for its abundant nature, safety, and biodegradability and as an ecofriendly alternative of synthetic polymers. Whey protein isolate and whey protein concentrate are the two major forms of whey protein involved in the formation of edible films and coatings. An edible whey film is a dry, highly interacting polymer network with a three-dimensional gel-type structure. Films/coatings made from whey proteins are colorless, odorless, flexible, and transparent with outstanding mechanical and barrier properties compared with polysaccharide and other-protein polymers. They have high water vapor permeability, low tensile strength, and excellent oxygen permeability compared with other protein films. Whey protein-based films/coatings have been successfully demonstrated in certain foods as vehicles of active ingredients (antimicrobials, antioxidants, probiotics, etc.), without considerably altering the desired properties of packaging films that adds value for subsequent industrial applications. This review provides an overview of the recent advances on the formation and processing technologies of whey protein-based edible films/coatings, the incorporation of additives/active ingredients for improvement, their technological properties, and potential applications in food packaging.

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.

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e Lactobacillus mucosae LM1, isolated from stool samples of a healthy piglet, displays good in vitro mucin adhesion and antimicrobial activity against pathogenic bacteria. To elucidate its antimicrobial effects and to find its epithelial cell and mucin adhesion genes, the genomic sequence of L. mucosae LM1 was investigated.L actobacillus mucosae, found in the mammalian gastrointestinal tract, has been shown to have the ability to adhere to mucosal surfaces (2,3,9). Previous reports have identified L. mucosae as having the ability to attach tightly to the epithelium of the human intestine and to produce antimicrobials and a biofilm when exposed to the physiological conditions of the gut (4). The adhesion of lactobacilli to gastrointestinal mucus makes them a good choice for probiotics since it increases their ability to colonize the gut efficiently, modulate the intestinal immune system, and inhibit pathogenic bacteria (1, 4, 9).L. mucosae LM1 was isolated from stool samples from a healthy piglet (6). Preliminary trials regarding the adhesion and antibacterial activity of L. mucosae LM1 demonstrated good mucin-binding activity in vitro and antibacterial activity against pathogenic bacteria. The genome of L. mucosae LM1 was determined using a Roche 454 GS FLX sequencer and Illumina GA IIx platform. All reads were assembled into 55 contigs by de novo assembly. The initial draft assembly was prepared from the libraries of 22,092,187 reads (950ϫ coverage) using Newbler Assembler 2.3 (Roche), CLC Genomics Workbench 4.8 (CLCbio), and CodonCode Aligner (CodonCode Co.). A functional annotation was performed by the Rapid Annotation using Subsystem Technology (RAST) server and BLASTP-based comparisons with the KEGG and COG databases.The draft genome of L. mucosae LM1 included 2,213,697 bp with a 45.87% GϩC content, 2,039 protein-coding genes, and 56 tRNA-encoding genes. Functions were assigned to 64.6% (1,318) of the total coding sequences; 8.7% (428) were found to be hypothetical proteins that are unique to this strain. A phylogenetic tree produced from the 16S rRNA genes revealed that strain LM1 is most closely related to L. mucosae CCUG 43169 (8). Likewise, 16S rRNA analysis showed strong homology to other Lactobacillus species with completed genomes, including Lactobacillus reuteri DSM 20016 (NCBI reference NC_009513.1), with 94% similarity, and Lactobacillus fermentum IF03956 (GenBank reference AP008937.1), with 95% similarity. The 16S rRNA gene sequence was extracted from whole-genome shotgun assemblies derived from the EzTaxon-e database (5).An analysis of the L. mucosae LM1 genome revealed that LM1 has a specific mucus-binding protein (mub) gene (LBLM1_04370), which showed 95% coverage and 93% similarity to the best-matched L. reuteri mub gene. The mucus-binding activity induced by this mub gene has antimicrobial effects through cell surface protection (7,8). Moreover, the L. mucosae LM1 genome includes a putative ABC transporter and adhesin-like protein (LBLM1_10110) with significant homology (100% coverage and 93...

Lactic acid bacteria were isolated from piglets and chicken and characterized. Lactic acid bacteria showing resistance to low pH and bile, adhesion to intestinal epithelium cells, and the inhibition of Escherichia coli and Salmonella spp. were identified as Lactobacillus acidophilus. L. acidophilus PF01 survived for 2 h in MRS broth adjusted to pH 2. L. acidophilus CF07 was less resistant than L. acidophilus PF01 to pH 2, but survived at pH 2.5 for 2 h. Both of isolates were able to grow in MRS broth containing 0.3% (w/v) bile, with L. acidophilus CF07 being more tolerant to bile than L. acidophilus PF01. L. acidophilus PF01 and CF07 adhered specifically to the duodenal and jejunal epithelium cells of piglet, and the cecal and duodenal epithelium cells of chicken, respectively. Both of isolates did not adhere to the epithelium cells of the various animal intestines from which they were isolated. When L. acidophilus was cultured with E. coli and Salmonella spp. in MRS broth, MRS broth containing 2% skim milk powder or modified tryptic soy broth at 37°C, L. acidophilus PF01 and CF07 inhibited the growths of E. coli K88 and K99, and S. enteritidis and S. typhimurium, respectively. Both of isolates were found to possess the essential characteristics of probiotic lactic acid bacteria for piglet and chicken. (Asian-Aust.

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