• Journal of Pharmaceutical Investigation
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• v.33 no.4
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• pp.273-279
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• 2003

Pancreatin is a enzyme mixture breaking down carbohydrates, proteins and lipids. Most pancreatin used in Korea is imported from foreign countries. However, guideline of each country for pancreatin produced from each country is different. Therefore, guideline for pancreatin imported from several countries, such as Europe, Japan and America, it is standardized to control its quality. Assay of enzyme activity for pancreatin in KP is similar to tat in JP, but it is significantly different from those in FP ad in USP. We measured pancreatin digestive activities of 17 commercial products. Activity assay of digestive enzymes, starch- and lipid-digestive enzymes, for pancreatin by KP method (including JP) was difficult compared to those by FIP ad USP methods. Particularly, activity assays of starch- and lipid-digestive enzymes by KP method were mistakable, ad varied in diluted samples than those by FIP. However, activity assay of protein-digestive enzyme by KP method was similar to that by FIP. Starch-digestive enzyme activities of 17 commercial pancreatins by KP method were lower 0.079-fold compared to those by FIP method. Their protein-digestive enzyme activities by KP method were higher 75.7-fold than those by FIP method. Their lipid-digestive enzyme activities by KP method were lower 0.234-fold compared to those by FIP method.

• Journal of Pharmaceutical Investigation
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• v.19 no.4
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• pp.203-212
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• 1989

A proteolytic enzyme was extracted from Sarcodon aspratus (Berk) S. Ito by percolation method. Proteolytic activity of the extracted proteolytic enzyme (SAP) was compared with several digestives containing proteolytic enzymes. Potency of SAP was higher than that of the other digestives except for protease. The optimum pH ranse of SAP was similar to that of pancveatin and protease. SAP was more stable than pancreatin and protease under various temperature, alkaline pH, and metal ions. Bovine serum albumin hydrolysing activity of SAP was equivalent to that of pancreatin and protease in small intestine of rats. SAP demonstrated lower adsorption to antacids than pancreatin and protease. Among the mixtures of SAP and several antacids, magnesium oxide-SAP showed the highest proteolytic activity.

• Food Science of Animal Resources
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• v.44 no.4
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• pp.885-898
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• 2024

Ovomucin (OM), which has insoluble fractions is a viscous glycoprotein, found in egg albumin. Enzymatic hydrolysates of OM have water solubility and bioactive properties. This study investigated that the immunostimulatory effects of OM hydrolysates (OMHs) obtained by using various proteolytic enzymes (Alcalase^®, bromelain, α-chymotrypsin, Neutrase^®, pancreatin, papain, Protamax^®, and trypsin) in RAW 264.7 cells. The results showed that OMH prepared with pancreatin (OMPA) produced the highest levels of nitrite oxide in RAW 264.7 cells, through upregulation of inducible nitric oxide synthase mRNA expression. The production of pro-inflammatory cytokines such as tumor necrosis factor-α and interleukin-6 were increased with the cytokines mRNA expression. The effect of OMPA on mitogen-activated protein kinase signaling pathway was increased the phosphorylation of p38, c-Jun NH2-terminal kinase, and extracellular signal-regulated kinase in a concentration-dependent manner. Therefore, OMPA could be used as a potential immune-stimulating agent in the functional food industry.

• KSBB Journal
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• v.18 no.4
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• pp.301-305
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• 2003

The study of pancreatin extraction was investigated by supercritical fluid process. Using supercritical carbon dioxide extraction with entrainer the purification of pancreatin was possible to remove lipids from Hog pancreas. To observe the optimum conditions different experimental variables were changed as pressure, temperature, flow rate of solvent and 0.25 mm of sample size were evaluated for effective removal of lipids. Ethanol and n-hexane were used as an entrainer with 5 mL/min. Increasing pressure at constant temperature the efficiency of the lipid removal in Hog pancreas was improved and the protein was concentrated without denaturalization, compared that of the control Hog pancreas. The most efficient conditions of lipid elimination were 17 MPa of pressure and 35$^{\circ}C$ of temperature and 0.25 mm of sample size.

• Current Research on Agriculture and Life Sciences
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• v.32 no.3
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• pp.149-154
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• 2014

It is already known that adzuki beans (Vigna angularis) are able to control appetite. Therefore, this study tested the proteins isolated from adzuki beans for their protease resistance and interaction with the intestinal mucosa. The major proteins from adzuki beans were found to be resistant to the digestive enzymes pepsin and pancreatin, and were identified using 2D-SDS-polyacrylamide gel electrophoresis and mass spectrometry. The major adzuki proteins were easily fractionated by treating the soluble protein extract with 10mM $CaCl_2$, and were found to contain lactotransferrin, a homologous protein to the dynein light chain domain, proteinase inhibitor, and proteins with unknown functions. From a tissue binding assay using mouse intestinal tissue sections, the major protein fraction showed weak, yet significant and specific binding to the mucosa layer of the small intestine. Thus, the current results suggest that adzuki proteins are resistant to digestive enzymes, which enables them to survive protease digestion in the intestinal tract, plus they may interact with the intestinal mucosa layer. Therefore, the molecules responsible for controlling appetite in adzuki beans are presumably protease-resistant proteins that interact with the intestinal mucosa or delay digestion in the digestive tract.

• Food Science of Animal Resources
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• v.33 no.4
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• pp.493-500
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• 2013

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.

• Journal of Nutrition and Health
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• v.6 no.4
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• pp.55-60
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• 1973

To determine the effects of condiments upon Proteinase Activity, condiments such as welsh onion, garlic, ginger, black pepper, red pepper, mi-won (glutamic acid natrium), sugar, mustard and horse-radish were ground by a homogenizer, and each of them was dosed by 0%, 1%, 5% and 10% into Pancreatin Solution of 0.2% for storage at the temperature of 15 degrees Cels. The Enzyme Solution thus obtained then was measured at a certain interval of time by the Fuld Gross Method, and the following results were obtained. 1) The condiments that kept Proteinase Action of Pancreatin checked below 75% were mustard, horse-radish, red pepper and welsh onion. The centrol power of welsh onion, in particular, became stronger as storage time became longer. 2) The condiments that kept Proteinase Action of Pancreatin checked below 50% were sugar, black pepper and ginger. 3) Mi-won and garlic showed a strong checking powor over Proteinase Action at an early stage of storage, but as time passed, their control power gradually diminished to naught. In short, it may be concluded that ail of the condiments used in this experiment demonstrated their checking power over Proteinase Action.

• Korean Journal of Food Science and Technology
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• v.30 no.5
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• pp.1128-1133
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• 1998

Extrusion cooking treatment was compared with autoclaving/cooling treatment for formation of enzyme resistant starch of high amylose corn starch (HACS). Effects of barrel temperature $(100^{\circ}C,\;120^{\circ}C,\;140^{\circ}C)$ and feed moisture content (25%, 35%, 45%) on extrusion processing in a co-rotating twin-screw extruder under fixed screw speed (100 rpm) were investigated by measuring enzyme resistant starch (RS) yield. RS yield were estimated by in-vitro pancreatin digestion method and enzymatic-gravimetric method using termamyl. Barrel temperature and yield of RS were negatively correlated and feed moisture content and yield of RS was positively correlated as determined by in-vitro pancreatin method. The highest yield (38.4%) of RS was obtained from HACS extrudate processed at the barrel temperature of $100^{\circ}C$ and the feed moisture content of 45%, while the yield of RS by 5 times of autoclaving/cooling was 25%. The yield of RS by in vitro pancreatin digestion method was 20.7% with high amylose corn starch and 8.2% with ordinary corn starch (CS), respectively, under the same extrusion condition (barrel temperature $120^{\circ}C$, feed moisture content 35%). At the same condition, the yields of RS by enzyme-gravimetric method were 14.6% with HACS and 6.8% with CS, respectively. The yield of RS increased during the storage at $4^{\circ}C$ for 4 weeks and the highest yield (60%) was obtained by the storage of HACS extrudates extruded at $100^{\circ}C$ and 45% feed moisture content.

• Applied Biological Chemistry
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• v.19 no.2
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• pp.70-74
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• 1976

In order to study the mechanism of biosynthesis of thyroid hormones, radioactive iodine was injected into the rats and thyroid glands were removed. Iodine compounds hydrolyzed by pancreatin viokase were separated by paper chromatography and analyzed by radioautography. Radioautograms showed that the uptake of iodine starts immediately and forms diiodotyrosine through monoiodotyrosine. Evidence supported the possibility that diiodotyrosine is a precursor of thyrosine and triiodothyronine is a degradation product of thyroxine. The rat administered propylthiouracil showed inorganic iodine concentration activity, while the binding activity was prevented.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.12 no.1
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• pp.276-280
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• 2011

This study investigated the activation conditions of pancreatic enzymes from porcine pancreas. Duodenum induced the activation of pancreatic protease and lipase in pancreas. When 10% duodenum was added to pancreatic juice and the mixture was incubated at $30^{\circ}C$ for 90 min or at $25^{\circ}C$ for 4 hrs, the activities of pancreatic protese and lipase reached the peak. When the pancreatin was prepared by sequential process of enzymatic activation at $25^{\circ}C$ for 4 hrs, centrifugation, acetone precipitation and freeze-drying, the specific activities of pancreatic protease, lipase and amylase were 136, 116 and 400 U/mg-protein, respectively. The protease, lipase and amylase activities of the prepared pancreatin were 5.4, 58.0 and 16.0 times higher than those of USP standard, respectively.