Curcuma longa L. (CL), a traditional medicinal plant, is well known as a functional food ingredient. The major component of CL is a curcumin of anthocyanin family that has multi-functions such as antimicrobial, anticancer, and antioxidant activity. In this study, fermented milk containing CL was prepared using a mixed strain culture (Bifidobacterium bifidus, Streptococcus thermophilus, Lactobacillus acidophilus), and its physicochemical properties were characterized. In addition, inflammatory cytokine-modulating effects of the fermented milk were also investigated. As regards the properties of fermented milk, the growth rate of lactic acid bacteria in fermented milk containing CL was found to be remarkably more rapid than control. During fermentation, caseins and whey proteins were observed to be partially hydrolyzed, and lactic acid and acetic acid were produced in larger amounts than in the control. The sensory score of fermented milk containing CL was lower than control, owing to its bitter taste and strong flavor. RAW 264.7 cells treated with CL fermented milk supernatant showed no cytotoxicity. Inflammatory cytokines such as tumor necrosis factor-alpha (TNF-α) and interleukin-6 (IL-6) were significantly produced by fermented milk with CL, compared to control. The secretion of nitric oxide (NO) from RAW 264.7 cells significantly increased relative to the control. Results from the present study suggested that CL could be used as a natural immunomodulating ingredient for making yogurts, beverages, and other products.Key words : Cytokine, fermented milk, inflammatory, lactic acid bacteria, Curcuma longa L.
: Degrees of hydrolysis by alkaline protease produced from Serratia marcescens S3-R1 is 3.95-6.30% of whey proteins during 5, 15, 30, 60, 90, 120,180, 240 min incubation at 40 °C. Proteolytic pattern of the whey proteins showed that various low molecular weight peptides were generated during the incubation periods. The biological function of in Raw 264.7 cells treated with whey protein hydrolytic peptides, anti-inflammatory effect showed exhibit in the expression of pro-inflammatory cytokines such as TNF-α, IL-6, COX-2 and iNOS by PCR analysis. COX-2 and iNOS gene expression inhibited in Raw 264.7 cells on whey protein hydrolysates below 3,000 dalton. The protease from Serratia marcescens S3-R1 showed a potential in production of low molecular weight whey protein hydrolysates which could be used for industrial application.
:The aim of this study was to produce enzymatic hydrolysis of α-LA, β-LG and BSA with alcalase for the possible application of hypoallergenic foods toward cow's milk allergenic infant. The molecular weights of most of the peptides in hydrolysates from α-LA, β-LG and BSA by alcalase were below 3,000 dalton. Antigenesity of α-LA, β-LG and BSA hydrolysates to rabbit anti-α-LA antiserum, β-LG antiserum and BSA antiserum were remarkably decreased by more than 10 -3 at 20% inhibitionrate. Antigenesity of polyvalent antigenic peptide in α-LA, β-LG and BSA hydrolysates to specific rabbit anti-α-LA antiserum, β-LG antiserum and BSA antiserum was determined by PCS test using guina-pig.Hydrolysates of α-LA, β-LG and BSA with less than 3,000 dalton did not show polyvalent antigenic reaction against rabbit antiserum. Hydrolysates of α-LA, β-LG and BSA could be a source for the manufacturing of hypoallergenic food.
:The aim of this study was to introduce a simple method for isolation of α-lactalbumin, β-lactoglobulin and bovine serum albumin from cow's milk, and peptides produced by enzymatic hydrolysis of α-lactalbumin, β-lactoglobulin and bovine serum albumin with alcalase. Whey protein were precipitated from whey by ammonium sulfate and, α -lactalbumin and β-lactoglobulin were isolated using Hi Prep 26/60 Sephacryl S-100 column gel filtration chromatography. Bovine serum albumin and β-lactoglobulin were isolated by Mono-Q 5/50 GL column anion exchange chromatography of the 50% Ammonium Sulfate-supernatant. Isolated whey proteins were hydrolyzed by proteolytic alcalase. Tricine SDS-PAGE and reverse-phase HPLC analyses revealed that almost hydrolyzed all the α-lactalbumin, β-lactoglobulin and bovine serum albumin with alcalase. Molecular weight of various peptides derived from alcalase hydrolysate were small molecular weight than 3.5 kDa.
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