• Journal of Microbiology and Biotechnology
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• v.6 no.4
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• pp.238-244
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• 1996

$\gamma$-Glutamyl transpeptidase ($\gamma$-GTP; EC 2.3.2.2) present in the culture filtrate of Bacillus sp. KUN-17 was purified 400-fold through a consecutive procedure including organic precipitation and column chromatography. The enzyme has an estimated molecular weight of 70, 000 and consists of hetero-subunits with molecular weights of 42, 000 and 22, 000. In vitro optimal conditions for those transfer and hydrolysis reactions appeared to be pH 7.0 at $50^{\circ}C$ and pH 8.4 at $40^{\circ}C$, respectively. The denatured enzyme recovered most of its $\gamma$-GTP activity by removing detergents such as sodium dodecyl sulfate (SDS) or urea with dialysis. The enzyme showed higher affinities against a number of amino acids as $\gamma$-glutamyl acceptors than glycylglycine in the following order: L-valine, L-methionine, L-glutamic acid or L-as-paragine, L-alanine. Also, it was shown that L-glutamine was the most suitable $\gamma$-glutamyl donor for the transfer reaction among those tested. Amino acids generally inhibited the enzyme activity for the transfer reaction, but not for the hydrolysis reaction.

• Preventive Nutrition and Food Science
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• v.20 no.3
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• pp.176-182
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• 2015

Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined. Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with $IC_{50}$ of 0.46 mg/mL, and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical absorbance capacity value of $457.6{\mu}M$ trolox equivalent/mg sample. Flavourzyme abalone protein hydrolysates (FAPH) also exhibited $H_2O_2$ scavenging activity with $IC_{50}$ of 0.48 mg/mL and $Fe^{2+}$+ chelating activity with $IC_{50}$ of 2.26 mg/mL as well as high reducing power. FAPH significantly (P<0.05) protected $H_2O_2$-induced hepatic cell damage in cultured hepatocytes, and the cell viability was restored to 90.27% in the presence of FAPH. FAPH exhibited 46.20% intracellular ROS scavenging activity and 57.89% lipid peroxidation inhibition activity in cultured hepatocytes. Overall, APH may be useful as an ingredient for functional foods.

• Journal of Environmental Science International
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• v.19 no.10
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• pp.1247-1256
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• 2010

Since biodiesel as bioenergy is defined as ester compounds formed by esterification of animal/vegetable oils, in this study three vegetable cooking oils (market, waste and refined waste ones) were esterified by reactions of alkali catalyst and immobilized enzyme. The fatty acid composition of the formed ester compounds was analyzed to investigate the feasibility of biodiesel production. By lipolysis (i.e, hydrolysis of Triglyceride (TG)), all three vegetable oils used in this study were found to produce Diglyceride (DG), Monoglyceride (MD) and Fatty acid ethylester (FAEE). However, the amount of produced FAEE (which can be used as an energy source) was in the increasing order of market cooking oil, waste one and refined waste one. With NaOH catalyst, FAEE was produced about 24.92, 17.63 and 11.31 % for the respective oils while adding Lipozyme TL produced FAEE about 43.54, 38.16 and 24.47 %, respectively. This indicates that enzyme catalyst is more effective than alkali one for transesterification. In addition, it was found that the composition of fatty acids produced by hydrolysis of TG was unchanged with alkali and immobilized enzyme reactions. Thus it can be expected that stable conditions remain in the course of mixing with gasoline whose composition is similar to that of the fatty acids.

• Preventive Nutrition and Food Science
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• v.14 no.4
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• pp.323-328
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• 2009

Cryotin F could be used for hydrolyzing shrimp byproducts into bioactive ingredients, which could be used as value-added products. The objective of this study was to investigate the optimum condition for antioxidative activities of the enzymatic hydrolysate produced with Cryotin F using response surface methodology with central composite rotatable design. Shrimp byproducts (shells and heads) were hydrolyzed with Cryotin F. The experimental ranges of the independent variables for 20 experimental runs were 28.2-61.8${^{\circ}C}$ reaction temperature, pH 6-10 and 0.5-5.5% enzyme concentration. The degree of hydrolysis for the reaction products was measured. Their antioxidative activities were measured using 1,1-diphenyl-2-picryl-hydrazyl (DPPH) scavenging activity and Fe-chelating activity. The experimental method with central composite rotatable design was well designed to investigate the optimum condition for biofunctional ingredients with antioxidative activities using Cryotin F because of their high R2 values of 0.97 and 0.95 for DPPH-scavenging activity and Fe-chelating activity, respectively. Change in enzyme concentration did not significantly affect their antioxidative activities (p<0.05). Both DPPH scavenging activity and chelating activity against Fe for the enzyme hydrolysates were more affected by the pH of enzyme hydrolysis than by their action temperature. DPPH-scavenging activity was higher at acidic pH than alkali pH, while chelating activity against Few was inversely affected. Hydrolysate of shrimp byproducts showed high antioxidative activities depending on the treatment condition, so the optimum treatment of enzymatic hydrolysate with Cryotin F and other proteases can be applied to shrimp byproducts (shells) and other protein sources for biofunctional ingredients.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.3
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• pp.340-348
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• 1993

Cross-synergistic interactions were evaluated with purified enzymes from Trichoderma viride and Penicillium funiculosum cellulase. Different synergistic patterns between enzyme components were observed. Exo-exo type synergism was found to be the most effective for degrading Avicel in all cases. Exo-endo type synergism was found to be slightly less effective. Extended hydrolysis of Avicel was carried out using mixtures of purified enzyme components with the crude cellulase from a different source. Addition of $\beta$-glucosidase from P. funiculosum cellulase to T. viride cellulase provided the great enhancement of Avicel hydrolysis. In addition, exoglucanase from T. viride cellulase was found to enhance P. funiculosum cellulase in degradation of Avicel. In conclusion, it was possible to enhance the hydrolysis of Avicel by altering the proportions of enzyme components by supplementing enzyme components from a different source. Different types of synergisms acted together to achieve maximum conversion.

• Journal of the Korean Wood Science and Technology
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• v.38 no.5
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• pp.429-438
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• 2010

In this study, effect of carbon source on the hydrolytic ability of the enzyme from Fomitopsis pinicola, a brown rot fungi, for lignocellulosic biomass were examined on two lignocellulosic biomasses (rice straw and wood) without any pretreatment. Cellulase activities of crude enzyme from F. pinicola, which was cultured on softwood mixture as a carbon source, were 19.10 U/$m{\ell}$ for endo-${\beta}$-1,4-gulcanase (EG), 36.1 U/$m{\ell}$ for ${\beta}$-glucosidase (BGL), 7.27 U/$m{\ell}$ for cellobiohydrolase (CBH), and 7.12 U/$m{\ell}$ for ${\beta}$-1,4 xylosidase (BXL). Softwood mixture as a carbon source in F. pinicola comparatively enhanced cellulase activities than rice straw. The optimal pH and temperature of the cellulase was identified to pH 5 and $50^{\circ}C$for the hydrolysis of rice straw. Under these condition rice straw was hydrolyzed to glucose by the cellulase up to $32.0{\pm}3.1%$ based on the glucan amount of the rice straw for 72 h, while the hydrolytic capability of commercial enzyme (Celluclast 1.5${\ell}$) from rice straw to glucose was estimated to $53.7{\pm}4.7%$ at the same experimental condition. In case of addition of Tween 20 (0.1% w/w, substrate) to the cellulase the hydrolysis of rice straw to glucose was enhanced to $38.1{\pm}2.0%$.

• Food Science of Animal Resources
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• v.22 no.1
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• pp.87-93
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• 2002

Angiotensiri-I converting enzyme(ACE) catalyst the removal of the C-terminal dipeptide from the angiotensin-I to give the angiotensin-II, a potent peptide that causes constriction of regulation of blood pressure. Recently, ACE inhibitor peptides have been isolated from enzymatic digests of food protein. The aim of this study was to identify bovine casein hydrolysates with ACE inhibitory properties in different enzymatic hydrolysis conditions. The casein were hydrolyzed neutrase, alcalase, protamax, flavourzyme, premed 192, sumizyme MP, sumizyme LP and pescalase alone and with an enzyme combination. Premed 192 produced ACE inhibitory peptides most efficiently. In order to ACE inhibitory peptide produced enzymatic hydrolysis condition were premed 192 added to casein ratio of 1:100(w/w), and incubated at 47$\^{C}$ for 12hrs. Casein hydrolysate gave 50% inhibition(IC$\_$50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.

• YAKHAK HOEJI
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• v.38 no.1
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• pp.12-19
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• 1994

Capsaicin(8-methyl-N-vanillyl-6-nonenamide) is the principal pungent component of Capsicum fruits. This work is directed to the capsaicin-hydrolyzing enzyme playing a key role in the rate limiting and critical step of capsaicin metabolism. In order to get precise information on the enzyme's subcellular location, rat liver homogenate was divided into six subcellular fractions by differential centrifugation technique: crude nuclear pellet, PNS(post nuclear supernatant) fraction, lysosomal pellet, cytosol, Tris wash fraction, micrisomes. Capsaicin-hydrolysing enzyme activity was analysed by high performance liquid chromatography(HPLC). This enzyme was found at the highest specific activity in the microsomal fraction and co-distributed with marker enzymes of the endoplasmic reticulum, NADPH-cytochrome c reductase and nucleoside diphosphatase. This is compatible with the result of ninhydrin color reaction of vanillylamine, primary metabolite of capsaicin hydrolysis, on thin layer chromatography(TLC). This enzyme is most active at pH $8.0{\sim}9.0$. Definite subcellular location of this enzyme will make it easy to proceed with further study.

• Journal of Korea Foresty Energy
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• v.20 no.2
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• pp.20-27
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• 2001

An effective method for production of glucose was developed using enzymatic hydrolysis of Suwon poplar by the cellulase. Enzymatic hydrolysis of wood is the reaction to produce glucose from wood using enzyme which derives from microorganism. Glucose can be transferred easily to ethanol by fermentation. Ethanol is the starting material for producing acetone, butanol, citric acid and lactic acid. The mechanism of the enzymatic hydrolysis of cellulose are reasonably explained in terms of the sequential action of three different types of enzymes, endo-cellulase, ex-cellulase, and $\beta$ -glucosidase. The goal of this work was to investigate the cellulose hydrolysis pretreated polar with various concentration NaOH, the crystallinity of cellulose, lignin contents and the degree of hydrolysis.

• Fashion & Textile Research Journal
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• v.18 no.6
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• pp.889-896
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• 2016

This study aims to evaluate the hydrolytic activity of a commercial nitrilase and optimize nitrilase treatment conditions to apply eco-friendly finishing on acrylic fabrics. To assess the possibility of hydrolyzing nitrile bonds in acrylic fabric using a commercial nitrilase, the amounts of hydrolysis products, ammonia and carboxylate ions, were measured. The treatment conditions were optimized via the amount of ammonia. The formation of carboxylate ions on the fabric surface was detected by X-ray photoelectron spectroscopy and wettability measurements. After nitrilase treatment, ammonia was detected in the treatment liquid; thus, nitrilase hydrolyzed the nitrile bonds in acrylic woven fabric. The largest amount of ammonia was released into the treatment liquid under the following conditions: pH 8.0, $40^{\circ}C$, and a treatment time of 5 h. The formation of carboxylate ions on the acrylic woven fabric surface by nitrilase hydrolysis was proven by the increased O1s content measuring of XPS analysis. From comparison of the results of nitrilase and alkaline hydrolysis, the white index and strength of the alkali-hydrolyzed acrylic fabric decreased, whereas those of the nitrilase-hydrolyzed samples were maintained. The nitrilase hydrolysis improved the sensitivity of acrylic fabrics to basic dye similarly to alkaline hydrolysis without the drawbacks of yellowing and decreased strength caused by alkaline hydrolysis.