• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.6
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• pp.783-788
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• 2010

The purpose of this study is to investigate the antioxidative activity and digestive enzyme inhibition of grape seed extract (GSE). The GSE was tested for its effect on various antioxidative potentials (scavenging activities of DPPH radical, superoxide anion radical and hydroxyl radical) and inhibitory effect of various digestive enzymes (trypsin, $\alpha$-chymotrypsin, $\alpha$-amylase, $\beta$-glucosidase and lipase). DPPH radical scavenging activity ($SC_{50}$, 50% scavenging concentration) of GSE was 4.76${\pm}$0.27 ppm while those of positive controls (EGCG and vitamin C) were 2.22${\pm}$0.12 ppm and 9.50${\pm}$0.72 ppm, respectively. $SC_{50}$ value of GSE against superoxide anion radical and hydroxyl radical were 3.82${\pm}$0.07 ppm and 803.23${\pm}$27.16 ppm, respectively. In addition, $IC_{50}$ values of GSE against trypsin, $\alpha$-chymotrypsin, $\alpha$-amylase, $\alpha$-glucosidase and lipase were 2.17${\pm}$0.59 ppm, 7.46${\pm}$1.25 ppm, 18.25${\pm}$3.54 ppm, 12.30${\pm}$1.12 ppm, and 653.23${\pm}$79.34 ppm, respectively. These results suggest that GSE may be useful for the prevention or treatment of obesity.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.20 no.5
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• pp.431-440
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• 1987

In order to develop a new type of food source for the effective utilization of fish protein, plastein reaction was applied to improve the functional properties of filefish protein. Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, pepsin, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper). Also, L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. And, General composition, yield, molecular weight, amino acid composition, color and IR spectrum of plasteins were measured. The protein, ash and lipid content of the plasteins were $72\~78\%,\;7.4\~11.8\%\;and\;0.3\~0.9\%$ respectively. The yield of plasteins were papain $55.0\%,\;pepsin\;47.6\%,\;\alpha-chymotrypsin\;38.3\%,\;protease\;23.6\%$, glutamic acid-incorporated plastein (Glu-Plastein) $35.0\%$, and leucine-incorporated plastein (Leu-plastein) $45.7\%$. The glutamic acid and leucine content in Glu-plastein and Leu-plastein were $38.7\%,\;41,7\%$, respectively, while the contents in the peptic filefish protein hydrolysate were $16.01\%\;and\;8.16\%$, respectively. The amino acid compositions were similar to that of the original filefish muscle protein. The major molecular weights of the peptic hydrolysate estimated by gel filteration were 2,000 and 310, and those of plasteihs were 21,000 and 4,900 for papain, 24,000 for pepsin, 18,500 for $\alpha-chymotrypsin$ 6,700 for protease, 24,000 for Glu-plastein and 17,000 for Leu-plastein. The structural changes in freeze-dried filefish meat, the FPC and hydrolysate were not observed on the IR spectrum. But plasteins showed amide I band in $1,600\~l,700cm^{-1}$ range and resulted in a strong band in $800\~850\;cm^{-1},\;700\~750\;cm^{-1}\;and\;650\~700\;cm^{-1}$. The amide I band of Glu-plastein was wider than those of other plasteins and had also a small band at $1,440\;cm^{-1}$.

• Korean journal of food and cookery science
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• v.17 no.1
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• pp.65-79
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• 2001

The effects of ${\alpha}$-chymotrypsin and trypsin treatments on the functional properties (degree of hydrolysis, solubility, and emulsifying capacity) of the soy protein isolate prepared from Jinpum soybean milk(JS milk) which has been developed as low lipoxidase-active soybean variety in Korea and extracted from commercially defatted soybean meal milk(DSM milk). The mixing ratios of JS milk to DSM milk were adjusted to 10:0, 7:3, and 5:5, respectively. The general quality attributes(yield, pH, titrable acidity, moisture contents, crude protein contents, color, textural properties, and sensory characteristics) of soybean cheese which has been prepared with the resulting soy protein hydrolysates were evaluated. Jinpum SPI was better subjected to trypsin than ${\alpha}$-chymotrypsin hydrolyses as indicated by better solubility and emulsifying capacity of the hydrolysates. The degree of hydrolysis and solubility of Jinpum SPI were higher than the soybean isolates from DSM milk. The increased ratios of DSM milk in the mixture resulted in the reduced yields and crude protein content along with the lowered titratable acidity while the pH values and moisture contents showed the opposite trends. In color characteristics, the increased amount of DSM milk brought about the significantly lower Hunter color reflectance values of lightness of the cheese products, along with the higher redness and total color difference value(ΔE). However, the enzyme treatment alone was not enough to cause any color differences. The increased ratios of DSM milk also caused the significantly lowered textural parameters such as hardness, adhesiveness and cohesiveness of the soybean cheese. Between the enzyme treatments, the ${\alpha}$-chymotrypsin treated samples resulted in the higher hardness and cohesiveness values of the products than those from the trypsin-treated ones. In organoleptic properties of the product, the better mouthfeel and overall quality scores were obtained from the trypsin treatments as compared with those from the ${\alpha}$-chymotrypsin ones. The mixing ratios of 10:0 and 7:3 were more favored than that of 5:5 as far as mouth-feel, yellowness and overall quality of the products were concerned. On the overall, the mixing ratio of 7:3(JS milk: DSM milk) and the trypsin treatment of the mixture was recommended for better manufacturing of high-quality soybean cheese.

• Korean Journal of Food Science and Technology
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• v.26 no.4
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• pp.436-441
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• 1994

To investigate the lowering effects of in vitro enzymatic hydrolysis by the treatment of chymotrypsin, trypsin, pancreatin, or protease from Aspergillus oryzae on the antigenicity of whey protein isolate (WPI) against rabbit anti ${\alpha}-LA$ antiserum, competitive inhibition ELISA (cELISA) and passive cutaneous anaphylaxis (PCA) test using guinea pig were performed. The results of cELISA showed that the monovalent antigenicity of the whey protein hydrolysates (WPH) to the antiserum was decreased to $10^{-2.5}-10^{-5.5}$ and less by the hydrolysis. The monovalent antigenicity of the WPH hydrolyzed by trypsin, or protease from Asp. nryzae was much lowered by the pretreatment of heat denaturation. The antigenicity of the WPH hydrolyzed by chymotrypsin, trypsin, or pancreatin was much lowered by the pretreatment of pepsin. Especially, the antigenicity of TDP (trypic hydrolysate with pretreatment of heat and pepsin) was found almost to be removed. However, there was not consistency between degree of hydrolysis(DH) and the monovalent antigenicity of the WPH. By the heterologous PCA it was found that all of the PGPH lost the polyvalent antigenicity regardless of the pretreatments although WPI and ${\alpha}-LA$ had the positive high antigenicity. The results suggested that the peptides derived from ${\alpha}-LA$ in WPH could bind specific antibodies but they could not induce allergy. Therefore, it was elucidated that the allergenicity of ${\alpha}-LA$ in whey protein could be destroyed easily by the enzymatic hydrolysis.

• Journal of the Korean Chemical Society
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• v.38 no.6
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• pp.449-455
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• 1994

In order to obtain the basic data for synthetic studies of bioactive peptide using enzyme, Kyotorphin(analgesic peptide) derivative was synthesized from Ac-Tyr-OH and $Arg-NH_2$ by $\alpha-chymotrysin$ in two phase system(organic phase and aqueous phase). In effect of organic solvent on Kyotorphin derivative synthesis from Ac-Tyr-OH(10 mM) and $Arg-NH_2$ (20 mM), the synthesis in ethyl acetate system of organic solvents was higher than those in other organic solvents (n-butanol, n-hexane, dichloromethane and chloroform). The optimal conditions for the synthesis are as follows: enzyme conc., 10 ${\mu}M;$ reaction pH, 7.0; reaction temp., $35^{\circ}C$ ; the ratio of organic phase volume/aqueous phase volume $(\alpha)$, 15. Under the optimal conditions, the yield was 70.2%, and the reaction achieved to equilibrium after 24 hrs.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1977.10a
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• pp.195.4-196
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• 1977

Trypsin에 대해서 비해물질을 생성하는 Streptomyces속 균주 AS 707을 선별하고 이 균주가 생성하는 물질의 작용성 및 제성질을 조사한 결과 본 저해물질은 열에 대해서 비교적 강하고 pH 처리에 대해서는 산성에서 중성에 걸쳐서는 안정하나 alkali성에서는 불안정했고 $\alpha-chymotrypsin과$ papain에 대해서도 저해작용을 하였으며 trypsin에 대한 저해양상은 mixed type이었다.(중략)

• Bulletin of the Korean Chemical Society
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• v.31 no.5
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• pp.1262-1266
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• 2010

In this study, we investigated the use of liquid crystals to selectively detect the activity of enzymes at interfaces decorated with oligopeptide-based membranes. We prepared a mixed monolayer of tetra(ethylene glycol)-terminated lipids and carboxylic acid-terminated lipids at the aqueous-liquid crystal (LC) interface. The 17 amino-acid oligopeptide SNFKTIYDEANQFATYK was then immobilized onto this mixed monolayer through N-hydroxysuccinimide-activation of the carboxylic acid groups. We examined the orientational behavior of nematic 4-cyano-4'-pentylbiphenyl (5CB) after conjugation of the 17 amino-acid oligopeptide with the mixed monolayer assembled at the interface. Immobilization of the oligopeptide caused orientational transitions in 5CB, with a change from homeotropic (perpendicular) to tilted alignment, which was primarily due to the reorganization of the monolayer. The orientation of the 5CB molecules returned to its homeotropic state after contacting the interface containing ${\alpha}$-chymotrypsin, which can cleave the immobilized oligopeptide. Control experiments confirmed that the enzymatic activity of ${\alpha}$-chymotrypsin triggered the ordering transitions in the LC. These results suggest that the LC can provide a facile method for selective detection of enzymatic activity.

• Microbiology and Biotechnology Letters
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• v.17 no.5
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• pp.529-532
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• 1989

A strain of Streptomyces sp. (YS-221-B) extracellularly produced an inhibitory substance for $\alpha$-D-Glucosidase. The substance was purified 96-fold from culture filtrate by dialysis, heat treatment, adsorption on active carbon, Bio-Gel P-10 and Sephadex G-75 column chromatography with yield of 9.2%. The substance was stable in pH range from 7.0 to 11.0 at 37$^{\circ}C$, and a treatment at 10$0^{\circ}C$ for 20 min diminished only 15% of the original activity. The inhibitor was not inactivated by the treatment of $\alpha$-, $\beta$-amylases, glucoamylases, trypsin and chymotrypsin but inactivated by pyoteases from Streptomyces griseus and Tritirachium album.

• Korean Journal of Food Science and Technology
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• v.28 no.1
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• pp.34-39
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• 1996

We examined the effects of crude hemicellulose, alcohol-insoluble hemicellulose, high molecular weight soluble polysaccharide (HMS-P : MW>10 kDa) and low molecular weight souble polysaccharide (LMS-P : MW<10 kDa) fraction isolated from buckwheat (raw, roast and steam) on digestive enzyme activity in vitro. The enzyme activities were measured after the polysaccharides-enzyme mixtures were incubated at $37^{\circ}C$ for 5 min. Crude hemicellulose, alcohol-insoluble hemicellulose and residue lowered ${\alpha}-amylase$ activity, whereas HMS-P and LMS-P had no inhibitory effect. All polysaccharides except LMS-P lowered lipase activity. Crude hemicellulose, alcohol-insoluble hemicellulose, residue and HMS-P showed a marked decrease of trypsin and chymotrypsin activity but LMS-P showed a slight decrease of them.

• Microbiology and Biotechnology Letters
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• v.37 no.4
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• pp.340-349
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• 2009

A CJ9 bacterial strain, which showed antifungal and antibacterial activities, was isolated from meju and identified as Bacillus polyfermenticus based on Gram staining, biochemical properties, as well as its 16S rRNA sequence. B. polyfermenticus CJ9 showed the antimicrobial activity against the various pathogenic molds, yeasts, and bacteria. The antibacterial activity was stable in the pH 5.0~9.0, but the activity was lost at $37^{\circ}C$ for 24 hr. The antifungal activity was stable in the pH range of 3.0~9.0 and reduced at $121^{\circ}C$ for 15 min, but antifungal activity was not completely destroyed. The antibacterial activity was completely inactivated by proteinase K, protease, trypsin, and $\alpha$-chymotrypsin. The antifungal activity was also completely inactivated by protease and $\alpha$-chymotrypsin, and reduced its activity by proteinase which indicated that the antifungal and antibacterial compounds have proteineous nature. The apparent molecular mass of the partially purified antifungal compound, as indicated by using the direct detection method in Tricine-SDS-PAGE, was approximately 1.4 kDa. The molecular mass of the antibacterial compound could not be determined because of its heat-liable characteristic.