• Preventive Nutrition and Food Science
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• v.7 no.2
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• pp.174-178
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• 2002

The influence of physical forms of gelatinized rice products on enzymatic hydrolysis in vitro and glycemic and insulinemic responses in normal subjects were studied. Densities of garaedu, bagsulgi, and cooked rice were 1.20, 1.18 and 1.11 g/mL, respectively, while moisture contents of garaeduk, bagsulgi, and cooked rice were 47.5, 43.1 and 66.0% (wt.), respectively. The highest initial rate of in vitro hydrolysis by porcine pancreatic $\alpha$-amylase was observed in bagsulgi followed by cooked rice and garaeduk. However, time for complete hydrolysis seemed to reach a plateau value. Postprandial glucose and insulin responses and satiety of rice products were studied in 12 normal subjects (mean age 23.2 $\pm$ 2.4 years, 6 men and 6 women). Postprandial serum glucose and insulin levels, after consumption of the rice products, reached a peak at 30 min. Garaeduk showed significantly less incremental responses for glucose (1627.5$\pm$134.9 mg.min/dL) and insulin (2041$\pm$287.0 uU.min/mL) than did bagsulgi for glucose (2407.4$\pm$208.3 mg.min/dL) and insulin (3582$\pm$264.4 uU.min/mL). Satiety responses to the rice products were not significantly different. Therefore, it can be concluded that garaeduk may be more beneficial in controlling postprandial hyperglycemia and hyperinsulinemia than bagsulgi. These results also suggest that physical properties of starch products, acquired by the specific processing methods, affect postprandial metabolism of carbohydrate foods.

• Korean Journal of Food Science and Technology
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• v.17 no.2
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• pp.60-64
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• 1985

To utilize microbial lipases for hydrolysis of milk fat, optimum reaction conditions and characteristics of enzymatic reactions of lipases originated from Rhizopus delemar, Mucor sp., and Candida cylindracea were investigated. Optimum pH and temperature were pH 5.6 and $45^{\circ}C$ for Rhizopus delemar lipase, pH7.5 and $35^{\circ}C$ for Mucor sp. lipase, and pH7.5 and $35^{\circ}C$ for Candida cylindracea lipase. Optimum lipase concentration and optimum substrate concentration were $600{\sim}800\;units/ml$ and 20% milk fat, regardless of their origin. Km values were 6.06% milk fat for Rhizopus delemar lipase, 7.69% for Mucor sp. lipase and 7.99% for Candida cylindracea lipase. Rate of lipid hydrolysis was Rhizopus delemar lipase>Mucor sp. lipase>Candida cylindracea lipase. As the reaction time was extended, liberation of short chain fatty acids was increased. After 8 hours reaction, capric acid content significantly increased with Candida cylindracea lipase, palmitic acid with Mucor sp. lipase and butyric acid with Rhizopus delemar lipase.

• Korean Chemical Engineering Research
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• v.54 no.6
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• pp.806-811
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• 2016

Organosolv pretreatment is the process to frationation of lignocellulosic feedstocks to enhancement of enzymatic hydrolysis. This process has advantages that organic solvents are always easy to recover by distillation and recycled for pretreatment. The chemical recovery in organosolv pretreatment can isolate lignin as a solid material and carbohydrates as fermentable sugars. For the economic considerations, using of low-molecular-weight alcohols such as ethanol and methanol have been favored. When acid catalysts are added in organic solvent, the rate of delignification could be increased. Mineral acids (hydrochloric acid, sulfuric acid, and phosphoric acid) are good catalysts to accelerate delignification and xylan degradation. In this study, the biomass was pretreated using 40~50 wt% ethanol at $170{\sim}180^{\circ}C$ during 20~60 min. As a results, the enzymatic digestibility of 2-stage pretreatment of rigida using 50 wt% ethanol at $180^{\circ}C$ was 40.6% but that of 1-stage pretreatment was 55.4% on same conditions, therefore it is shown that the pretreatment using mixture of the organosolv and catalyst was effective than using them separately.

• Applied Chemistry for Engineering
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• v.5 no.4
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• pp.681-697
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• 1994

The enzymatic hydrolysate of gelatin extracted from fish skin was fractionated and recycled through the membrane reactor according to the molecular weight for the purpose of using as functional material. In addition, the enzymatic hydrolysis conditions of gelatin, enzyme stability by membrane and mechanical shear, and effect on the long-term operational stability of the recycle membrane reactor were investigated. Using the pH-drop technique, Alcalase, pronase E and collagenase were identified as the most suitable enzymes for the hydrolysis of fish skin gelatin. The optimum hydrolysis conditions in the 1st-step membrane reactor(1st-SMR) by Alcalase were enzyme concentration 0.2mg/ml, substrate-to-enzyme ratio(S/E) 50(w/w), $50^{\circ}C$, pH 8.0, reaction volume 600ml and flow rate 6.14ml/min. In the 2nd-SMR by pronase E were enzyme concentration 0.3mg/ml, S/E 33(w/w), $50^{\circ}C$, pH 8.0, reaction volume 600ml and flow rate 6.14ml/min. In the case of 3rd-SMR, enzyme concentration 0.1mg/ml, S/E 100(w/w), $37^{\circ}C$, pH 7.5, reaction volume 600ml and flow rate 10ml/min. Decreased enzyme activities by mechanical shear and membrane were 30% and 15% in the 1st-SMR, were 14% and 5% in the 2nd-SMR, and 18% and 8% in the 3rd-SMR, respectively. Under the optimum conditions, the degree of hydrolysis in the 1st, 2nd and 3rd-SMR were 3.5%(Kjeldahl method, 87%), 3.1%(77%) and 2.7%(70%), respectively. The productivity of hydrolysate in the continuous three-step membrane reactor was 430mg per enzyme(mg) for 10 times of volume replacements.

• KSBB Journal
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• v.13 no.2
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• pp.147-154
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• 1998

Enzymatic hydrolysis using an immobilized enzyme was carried out to produce chitosan oligosaccharides (COSs) from chitosan effectively. Chitosanase was immobilized on eight different carriers by physical adsorption. The enzyme immobilized on chitin had higher activity than those immobilized on the other carriers in spite of its lower adsorption. The activity of chitin-immobilized enzyme was more than 90% of the original activity. Optimal temperature of the immobilized enzyme increased by about $15^{\circ}C$ and its thermostability was excellent in relatively wide range of temperature. But its effects of pH did not improve compared to the free enzyme. The immobilized enzyme produced 153 mg/g chitosan of the reducing sugar for 3hrs of hydrolytic incubation time. The total content of higher oligomers, tetramer to hexamer, among amount of total COSs obtained for 2hrs was more than 90%. In kinetic parameters for both enzymes, immobilized enzyme showed lower affinity for substrate and reaction rate than free enzyme, however, no reduction of the rate for high substrate concentrations. Consequently, chitin-immobilized could effectively hydrolyse chitosan and produce the higher COSs without activity decrease in comparison with the free enzyme.

• Food Science of Animal Resources
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• v.31 no.5
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• pp.663-667
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• 2011

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

• Journal of the Korean Wood Science and Technology
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• v.14 no.3
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• pp.23-29
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• 1986

Alakline peroxide pretreatment for the delignification of poplar wood was performed. sinceit is a simple and efficent method for enhancing the enzymatic digestibility of wood residues. Approximately one-half of their lignin and most of the hemicellulose present in poplar wood were removed when the wood sawdust was reacted at 25$^{\circ}C$ for 100 hrs in an alkaline solution (pH 11.5) of 1% peroxide. The rate of decomposition as well as the saccharification efficiency were enhanced up to 350% and 260% respectively in comparision with those of the controll. This enhancement is comparable with that pretreated with 1% sodium hydroxide and 20% peracetic acid successively. The advantages of alkaline peroxide as delignifying agents against other chemicals were also discussed.

• Food Science and Preservation
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• v.22 no.2
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• pp.297-302
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• 2015

Calcium is one of the essential mineral for the humans due to its crucial physiological functions in the body. Calcium deficiency results in many diseases, such as osteoporosis. Therefore, calcium supplements are available as a functional food. However, most calcium supplements in the market have a limitation due to poor absorption and low bioavailability. Thus, calcium-chelated peptides for improving the absorption rate of calcium have been isolated from foods including porcine meat and bone meal (MBM), and mussel using the enzymatic hydrolysis of their protein. The hydrolysates of food were ultra-filtered in order to obtain small peptides less than 3 kDa and the Ca-binding peptides were isolated via the anion exchange chromatography. The binding activity and concentration of Ca-binding pepetides were determined. In particular, the MBM and mussel protein hydrolysates were fractionated by mono Q and Q-Sepharose, respectively. As a result, among the fractions, the fractions of MBM F2 and mussel F3 showed the highest Ca-binding activity. These results suggest that MBM and mussel protein hydrolysates can be used as calcium supplements.

• Food Science and Preservation
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• v.23 no.5
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• pp.753-757
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• 2016

In this study, enzyme (thermoase) hydrolysis was applied to the porcine blood order to increase the iron content and solubility. It was confirmed that content of iron was increase up to 158.11 mg/100 g porcine powders after 0.2% thermoase treatment at $60^{\circ}C$ during 4 hr. The solubility of porcine blood powders was higher than other enzyme (various protease), temperature, reaction time. This optimized conditions were also worked to the in vitro iron bioavailability rate increasement, the bioavailability of hydolyzed porcine powders was 3-fold higher than that of an iron supplement on the market. These results indicate the possibility of porcine blood powder in iron supplements market as natural material. Also utilizing of reduced porcine blood will be possible to improve environmental issues.

• Food Science of Animal Resources
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• v.42 no.5
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• pp.800-815
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• 2022

This study aimed to obtain high Fischer's ratio oligopeptides from goat whey (HFO) and investigate antioxidant property of it. Hydrolysis of goat whey was done with the approach of sequential digestion of pepsin and flavourzyme. With the adsorption of aromatic amino acids by activated carbon, HFO with a Fischer's ratio of 27.070 and a molecular weight of 200-1,000 Da were obtained, and the branched-chain amino acids accounted for 22.87%. Then the antioxidant activity of HFO was evaluated. At the concentrations of 2.0 mg/mL and 0.50 mg/mL, HFO scavenged 77.27% and 99.63% of 1,1-diphenyl-2-picrylhydrazyl and 3-ethylbenzthiazoline-6-sulphonate free radicals respectively. The scavenging rate of HFO against hydroxyl radicals reached 92.31% at the concentration of 0.25 mg/mL. Animal experiments demonstrated that HFO could moderate the changes of malondialdehyde, superoxide dismutase and glutathione peroxidase caused by CCl₄-induced oxidative stress in vivo. This study indicated that HFO from goat whey was capable of oxidation resistance both in vivo and in vitro, which provided a scientific basis for the high-value processing and application of goat milk whey.