Myoung Soo Nam

Bioactive Peptides in Milk and Dairy Products: A Review.

Functionally and physiologically active peptides are produced from several food proteins during gastrointestinal digestion and fermentation of food materials with lactic acid bacteria. Once bioactive peptides (BPs) are liberated, they exhibit a wide variety of physiological functions in the human body such as gastrointestinal, cardiovascular, immune, endocrine, and nervous systems. These functionalities of the peptides in human health and physiology include antihypertensive, antimicrobial, antioxidative, antithrombotic, opioid, anti-appetizing, immunomodulatory and mineral-binding activities. Most of the bioactivities of milk proteins are latent, being absent or incomplete in the original native protein, but full activities are manifested upon proteolytic digestion to release and activate encrypted bioactive peptides from the original protein. Bioactive peptides have been identified within the amino acid sequences of native milk proteins. Due to their physiological and physico-chemical versatility, milk peptides are regarded as greatly important components for health promoting foods or pharmaceutical applications. Milk and colostrum of bovine and other dairy species are considered as the most important source of natural bioactive components. Over the past a few decades, major advances and developments have been achieved on the science, technology and commercial applications of bioactive components which are present naturally in the milk. Although the majority of published works are associated with the search of bioactive peptides in bovine milk samples, some of them are involved in the investigation of ovine or caprine milk. The advent of functional foods has been facilitated by increasing scientific knowledge about the metabolic and genomic effects of diet and specific dietary components on human health.

Upregulation and secretion of macrophage inhibitory cytokine-1 (MIC-1) in gastric cancers

BACKGROUND Macrophage inhibitory cytokine-1 (MIC-1), a distant member of the transforming growth factor (TGF)-beta superfamily, has been reported to be upregulated and secreted from several cancers. We examined MIC-1 expression and secretion in gastric cancers. METHODS MIC-1 mRNA and protein levels in cancer tissues and cell lines were analyzed by RT-PCR and Western blot. MIC-1 expression in cancer tissues and its secretion in serum were analyzed using immunohistochemistry and ELISA. RESULTS MIC-1 was significantly upregulated in gastric cancer tissues and cell lines. MIC-1 was secreted from gastric SNU620 cells and its levels in the serum of cancer patients were 10-fold higher than those of healthy controls. In addition, the staining of MIC-1 expression was strongly increased in metastatic gastric cancers. CONCLUSIONS MIC-1 was obviously overexpressed in gastric cancers and MIC-1 secretion into blood may be useful for the prediction of gastric cancer progression.

Saponins, especially platycodin D, from Platycodon grandiflorum modulate hepatic lipogenesis in high-fat diet-fed rats and high glucose-exposed HepG2 cells.

AMP-activated protein kinase (AMPK) plays a central role in controlling hepatic lipid metabolism through modulating the downstream acetyl CoA carboxylase (ACC) and sterol regulatory element-binding protein-1c (SREBP-1c) pathway. Saponins, particularly platycodin D, from the roots of Platycodon grandiflorum (Changkil saponins, CKS) have a variety of pharmacological properties, including antioxidant and hepatoprotective properties. The aim of this study was to investigate the effects of CKS on hepatic lipogenesis and on the expression of genes involved in lipogenesis, and the mechanisms involved. CKS attenuated fat accumulation and the induction of the lipogenic genes encoding SREBP-1c and fatty acid synthase in the livers of HFD-fed rats and in steatotic HepG2 cells. Blood biochemical analyses and histopathological examinations showed that CKS prevented liver injury. CKS and platycodin D each increased the phosphorylation of AMPK and acetyl-CoA carboxylase in HFD-fed rats and HepG2 cells. The use of specific inhibitors showed that platycodin D activated AMPK via SIRT1/CaMKKβ in HepG2 cells. This study demonstrates that CKS or platycodin D alone can regulate hepatic lipogenesis via an AMPK-dependent signalling pathway.

Purification, characterization, and properties of an alkaline protease produced by Serratia marcescens S3‐R1 inhabiting Korean ginseng rhizosphere

BACKGROUND An alkaline protease produced by the Serratia marcescens S3-R1 which inhabits in the Korean ginseng rhizosphere was investigated. The purposes of this study were to characterize and purify the bacterial enzyme by four different purification steps: precipitation of enzyme fraction by ammonium sulfate, loading the enzyme pellets on a DEAE-Sepharose anion-exchange chromatograph, separation of the fraction containing enzyme activity by fast protein liquid Mono Q chromatography and identification of the single-band fraction by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and then quantification of the single-band fraction by reverse-phase high-performance liquid chromatography. RESULTS The molecular weight of the purified protease was estimated as 50 308 Da by matrix-assisted laser desorption ionization time-of-flight analysis. The N-terminal amino acid sequence of the protease was identified as Ala-Val-Thr-Ile-Glu-Asp-Ala-Val-Asp-Asp, and the enzyme belongs to the metalloprotease family. The optimal activities of the protease occurred at pH 7-9 and a temperature 40 °C. The ranges of pH and thermal stability of the enzyme were at 7-10 and 30-40 °C, respectively. CONCLUSION The alkaline protease was successfully purified and characterized from the bacterium Serratia marcescens S3-R1, which has potential for industrial application, including milk protein hydrolysates.

Fermentation Properties and Inflammatory Cytokines Modulating of Fermented Milk with Curcuma longa L Powder

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.

Characteristics of α-Amylase and Protease Produced from Bacillus amyloliquefacies CNL-90 Isolated from Malt Grain

A bacterium, identified as Bacillus amyloliquefacies CNL-90 using 16S rDNA analysis, was isolated from malt grain. The optimal activities of its α-amylase and protease were observed at pH 6 and 60 , and at pH 6 and 50C, respectively although their activities remained stable at pH 7 and 40 for α-amylase and at pH 7 and 50 for protease. After solid-state fermentation of B. amyloliquefacies CNL-90 on wheat bran for 72hr or 144hr, the α-amylase and protease activities were 170,000 and 290,000 units/kg, and 290,000 and 310,000 units/kg, respectively. The viable bacterial cell counts were 1.5 × 10 9 CFU/g and 2.2 × 10 9 CFU/g at 72hr and 144hr of the solid-state fermentation, respectively. A feeding trial with a total of 127 piglets was also conducted. The animals were divided into two groups: an experimental group fed with the fermented product (63 piglets) and a control group (64 piglets). The growth rate of the experimental group was 6.66% higher than that of the control group (P<0.05). The results of this study indicate that the α-amylase and protease from B. amyloliquefacies CNL-90 can be used for industrial applications due to their activity in production of carbohydrate hydrolysates. (Key words : Bacillus amyloliquefacies CNL-90, α-amylase, Protease, Growth rate)

Functional Characteristics of Enterococcus faecium SA5 and Its Potential in Conversion of Ginsenoside Rb1 in Ginseng

본 연구는 몽골 마유로부터 분리한 유산균 Enterococcus faecium SA5의 이화학 특성을 파악하고 유산균 E. faecium SA5의

Thymic Stromal Lymphopoietin Induction Is Mediated by the Major Whey Proteins α-Lactalbumin and β-Lactoglobulin through the NF-κB Pathway in Immune Cells

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Effects of Psychrotrophic Bacteria, Serratia liquefaciens and Acinetobacter genomospecies 10 on Yogurt Quality

-glucosidase의 활성과 이를 통한 ginsenoside 전환을 확인하는 것을 목표로 진행되었다. E. faecium SA5는 내산성, 내담즙성을 나타내었으며 4종의 병원성 미생물(Salmonella typhimuriu...

Characterization of Paenibacillus sp. MBT213 Isolated from Raw Milk and Its Ability to Convert Ginsenoside Rb1 into Ginsenoside Rd from Panax ginseng

α-Lactalbumin and β-lactoglobulin are two major whey proteins that specifically bind immunoglobulin E and are suspected as major allergens causing cows milk allergy (CMA). Recent studies have shown that thymic stromal lymphopoietin is a critical factor linking at the interface of the body and environment to the T-helper 2 response. However, it is not known whether thymic stromal lymphopoietin expression is changed by α-lactalbumin and β-lactoglobulin in immune cells. Using RT-PCR and ELISA, the present study was conducted to examine if intravenous injection of α-lactalbumin and β-lactoglobulin increased pro-inflammatory cytokines, T-helper 2 cytokines, and thymic stromal lymphopoietin expression in several immune cells, including macrophages, mast cells, and keratinocytes. Results showed that α-lactalbumin and β-lactoglobulin induced thymic stromal lymphopoietin, interleukin-6, and tumor necrosis factor-α expression. It was concluded that the allergenicity of α-lactalbumin and β-lactoglobulin may be attributed to thymic stromal lymphopoietin induction, T-helper 2 cytokines, and pro-inflammatory cytokines.