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Antioxidant Activity of Porcine Skin Gelatin Hydrolyzed by Pepsin and Pancreatin
Chang, Oun Ki,Ha, Go Eun,Jeong, Seok-Geun,Seol, Kuk-Hwan,Oh, Mi-Hwa,Kim, Dong Wook,Jang, Aera,Kim, Sae Hun,Park, Beom-Young,Ham, Jun-Sang Korean Society for Food Science of Animal Resource 2013 한국축산식품학회지 Vol.33 No.4
Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical products. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethylbenzothiazoline- 6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absorbance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electrophoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest values after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation, that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was $87.8{\mu}M$, whereas $14.5{\mu}M$ GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORACFL assay, antioxidant activity corresponding to $45.7{\mu}M$ of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.
Antioxidant Activity of Porcine Skin Gelatin Hydrolyzed by Pepsin and Pancreatin
Oun Ki Chang,Go Eun Ha,Seok Geun Jeong,Kuk Hwan Seol,Mi Hwa Oh,Dong Wook Kim,Ae Ra Jang,Sae Hun Kim,Beom Young Park,Jun Sang Ham 한국축산식품학회 2013 한국축산식품학회지 Vol.33 No.4
Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical products. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethylbenzothiazoline- 6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absorbance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electrophoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest values after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation, that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was 87.8 μM, whereas 14.5 μM GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORACFL assay, antioxidant activity corresponding to 45.7 μM of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.
Novel Antioxidant Peptide Derived from the Ultrafiltrate of Ovomucin Hydrolysate
Chang, Oun Ki,Ha, Go Eun,Han, Gi-Sung,Seol, Kuk-Hwan,Kim, Hyoun Wook,Jeong, Seok-Geun,Oh, Mi-Hwa,Park, Beom-Young,Ham, Jun-Sang American Chemical Society 2013 Journal of agricultural and food chemistry Vol.61 No.30
<P>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.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jafcau/2013/jafcau.2013.61.issue-30/jf4013778/production/images/medium/jf-2013-013778_0003.gif'></P>
장운기 ( Oun Ki Chang ),설국환 ( Kuk Hwan Seol ),김민경 ( Min Kyung Kim ),한기성 ( Gi Sung Han ),정석근 ( Seok Geun Jeong ),오미화 ( Mi Hwa Oh ),박범영 ( Beom Young Park ),함준상 ( Jun Sang Ham ) 한국유가공기술과학회 2012 한국유가공기술과학회지 Vol.30 No.2
Lactic acid bacteria (LAB) have been used as starter cultures in the manufacturing processes of fermented dairy products such as cheese and yogurt. LAB have a proteolytic system to use the nitrogen source from milk for their growth. The proteolytic system involved in casein utilization provides cells with essential amino acids during growth in milk and is also of industrial importance, because of its contribution to the development of the organoleptic properties such as flavor of fermented milk products. In the most extensively studied LAB, Lactococcus lactis, the main features of the proteolytic system comprise 3 groups. The first is proteinase, which initially cleaves the milk protein to peptides. The second group consists of transport systems for the internalization of oligopeptides, which are involved in the cellular uptake of small peptides and amino acids. The third group, peptidases in the cell, cleaves peptides into smaller peptides and amino acids. This review is to provide the information about the proteolytic system of LAB.
장운기 ( Oun Ki Chang ),정석근 ( Seok Geun Jeong ),한기성 ( Gi Sung Han ),설국환 ( Kuk Hwan Seol ),박범영 ( Beom Young Park ),함준상 ( Jun Sang Ham ) 한국유가공기술과학회 2013 Journal of Dairy Science and Biotechnology (JMSB) Vol.31 No.1
Mare milk is gaining importance because of its nutritional characteristics and therapeutic properties, which enable its use as part of the diet of the elderly, convalescents, and newborn infants. This review describes the functional and bioactive components of mare milk, such as proteins, carbohydrates, and lipids, and the characteristics such as acidification and released free amino acids of fermented mare milk. The protein profile of mare milk differs from that of bovine milk but is similar to that of human milk. The salt and lactose content in mare`s milk is similar to that in human milk, but mare`s milk has a significantly lower content of fat. Whey protein concentration is higher and casein content is much lower in mare milk than in bovine milk. These health-promoting properties indicate that mare milk and its derivatives could become valuable foods for elderly consumers in the form of probiotic beverages. Protein allergies related to and the potential industrial applications of mare milk have also been discussed in comparison with those of bovine milk. Although mare milk has diverse advantages if used as a nutritional food and has positive effects on health, further studies are required to enable its use as a complete substitute for human milk or as a health food.
Go Eun Ha,Oun Ki Chang,Gi Sung Han,Jun Sang Ham,Beom Young Park,Seok Geun Jeong 한국축산식품학회 2015 한국축산식품학회지 Vol.35 No.3
Milk proteins have many potential sequences within their primary structure, each with a specific biological activity. In this study, we compared and investigated the bioactivities of hydrolysates of the domestic (A, B) and imported (C, D) skim milk powders generated using papain digestion. MALDI-TOF analysis revealed that all milk powder proteins were intact, indicating no autolysis. Electrophoretic analysis of hydrolysates showed papain treatment caused degradation of milk proteins into peptides of various size. The antioxidant activity of the hydrolysates, determined using 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and total phenolic contents (TPC) assays, increased with incubation times. In all skim milk powders, the antioxidant activities of hydrolysates were highest following 24 h papain treatment (TPC: A, 196.48 μM GE/L; B, 194.52 μM GE/L; C, 194.76 μM GE/L; D, 163.75 μM GE/L; ABTS: A, 75%; B, 72%; C, 72%; D, 57%). The number of peptide derived from skim milk powders, as determined by LC-MS/MS, was 308 for A, 283 for B, 208 for C, and 135 for D. Hydrolysate A had the highest antioxidant activity and the most potential antioxidant peptides amongst the four skim milk powder hydrolysates. A total of 4 β-lactoglobulin, 4 αs1-casein, and 56 β-casein peptide fragments were identified as potential antioxidant peptides in hydrolysate A by LC-MS/MS. These results suggest that domestic skim milk could have applications in various industries, i.e., in the development of functional foods.