• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.30 no.3
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• pp.15-21
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• 1998

Crude enzymes of Trichoderma viride and Phanerochaete chrysosporium were evaluated for their effect to brightness and physical properties of recycled pulp from newspaper and corrugated container board. The brightness of recycled pulp from newspaper increased with crude enzymes from Trichoderma viride and Phanerochaete chrysosporium. The brightness of recycled pulp of corrugated container board increased with crude enzyme from Phanerochaete chrysosporium, but decreased with crude enzyme from Trichoderma viride. The Δbrightness with chemical bleaching of crude enzyme treated pulp was lower than that of heat killed enzyme treated pulp, but the final brightness of pulp was increased. Modification of recycled paper with crude enzymes can result in a substantial increase in physical properties with little no loss in pulp freeness.

• The Korea Journal of Herbology
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• v.22 no.4
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• pp.29-34
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• 2007

Objective : Kyenegum(Galli Stomachichum Corium) has been popularly used long as the digestive. The purpose of this study was to investigate the enzymatic characteristic of Kyenegum crude enzyme. Methods : To evaluate of the enzymatic characteristic of Kyenegum, we examined the activity of Kyenegum crude enzyme from optimum solvent, optimum temperature and pH of crude Kyenegum extract. Futhermore, we examined the effects of NaCI and acidity of crude Kyenegum extract. Results : The Kyenegum was composed with crude protein about 20%, crude lipid 2%. The optimum Kyenegum dry condition, optimum extract solvent, optimum temperature and optimum pH were $4{\sim}6$ hours at $60^{\circ}C$, commercial apple vinegar, $50^{\circ}C$ and 2.0. Conclusion : The result suggests that the Kyenegum crude enzyme extract very strong enzyme in temperature, NaCl and acidity, respectively.

• Journal of Microbiology and Biotechnology
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• v.19 no.7
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• pp.666-674
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• 2009

An electrochemical bioreactor (ECB) composed of a cathode compartment and an air anode was used in this study to characterize the ethanol fermentation of Zymomonas mobilis. The cathode and air anode were constructed of modified graphite felt with neutral red (NR) and a modified porous carbon plate with cellulose acetate and porous ceramic membrane, respectively. The air anode operates as a catalyst to generate protons and electrons from water. The growth and ethanol production of Z. mobilis were 50% higher in the ECB than were observed under anoxic nitrogen conditions. Ethanol production by growing cells and the crude enzyme of Z. mobilis were significantly lower under aerobic conditions than under other conditions. The growing cells and crude enzyme of Z. mobilis did not catalyze ethanol production from pyruvate and acetaldehyde. The membrane fraction of crude enzyme catalyzed ethanol production from glucose, but the soluble fraction did not. NADH was oxidized to $NAD^+$in association with $H_2O_2$reduction, via the catalysis of crude enzyme. Our results suggested that NADH/$NAD^+$balance may be a critical factor for ethanol production from glucose in the metabolism of Z. mobilis, and that the metabolic activity of both growing cells and crude enzyme for ethanol fermentation may be induced in the presence of glucose.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.1
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• pp.122-126
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• 2004

A digestion trial in vitro was conducted to study effects of supplementation of NSP (non-starch polysaccharides) degrading enzyme (feed grade) on cell wall degradation and digestibility of nutrients in barley. The slices of barley were soaked in distilled water with or without 0.15% non-starch polysaccharides degrading enzyme. Microscopic examination of the slices showed that the endosperm cell wall of barley was completely degraded by the non-starch polysaccharides degrading enzyme. The residues and supernatant of digesta in vitro were separated by filtration with 0.1 mm nylon fabric. The residues were used for measurement of crude protein, crude fat, crude fiber, and moisture. The supernatant was used for determination of viscosity, as well as amino-nitrogen and glucose content. The results showed that compared with the control, the amino-nitrogen and glucose content of the supernatant increased by 17.58% (p<0.05) and 10.26% (p<0.05), respectively, while viscosity did not change. Enzyme supplementation increased the digestibilities of dry matter, crude protein, nitrogen-free extract, crude fat and crude fiber of barley by 18.1% (p<0.05), 20.3% (p<0.05), 16.4% (p<0.05), 26.9% (p<0.05) and 30.0% (p<0.05), respectively. The present study suggests that cell wall hydrolysis may contribute to improved nutrient digestion in vivo when non-starch polysaccharides degrading enzymes are fed to swine.

• Journal of the Korean Society of Food Culture
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• v.14 no.5
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• pp.455-460
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• 1999

In order to establish the processing condition of salt-fermented liquefaction of sardine (Sardinops melanoslicta), effect of temperature, pH value, and concentration of salinity on crude enzyme activity of sardine viscera were investigated. The optimum temperature range of crude enzyme activity in sardine viscera was $45{\sim}50^{\circ}C$ and the optimum pH value of it was 9.8. According to the concentration of salinity increased the crude enzyme activity in sardine viscera decreased. The relationship between concentration of salinity (X) and the crude enzyme activity (Y) in sardine viscera is shown as follows; Y=-0.01363X+0.7676 (r=-0.88). For the purpose of processing conditions of rapid- and low salt-fermented liquefaction of sardine, changes of viable cell count, histamine content, and volatile basic nitrogen (VBN) in the chopped whole sardine with 8% NaCl during preheating process at $40^{\circ},\;45^{\circ}$ and $50^{\circ}C$ for 48 hrs were analyzed. During preheating, initial viable cell counts of chopped whole sardine were $10^{4-7}/g$, but they decreased $10^{1-5}/g$ after 48 hrs. Histamine contents during preheating process at $40^{\circ}\;and\;45^{\circ}C$ were gradually increased, whereas at $50^{\circ}C$ were almost the same level after 48 hrs. VBN contents were continuously increased during preheating, but preheating at $50^{\circ}C$ samples were lower level than that of $40^{\circ}\;and\;45^{\circ}C$ ones. For the purpose to accelerate the fermentation and liquefaction of chopped whole sardine, preheating at optimum temperature of crude enzyme activity for 48 hrs was useful processing method and the contents of viable cell count, histamine, and VBN were safety level for food sanitation.

• Journal of Microbiology and Biotechnology
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• v.32 no.4
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• pp.430-436
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• 2022

Platycosides, Platycodi radix (Platycodon grandiflorus root) saponins, are used as food supplements and exert diverse pharmacological activities. Deglycosylation of saponins enhances their biological efficacy, and deglycosylated platycosides are produced mainly through enzymatic hydrolysis. However, the types of available deglycosylated platycosides remain limited because of a lack of hydrolyzing enzymes that can act on specific glycosides in glycosylated platycosides. In this study, a crude enzyme from Aspergillus tubingensis converted platycoside E (PE) and polygalacin D₃ (PGD3) into deglucose-apiose-xylosylated (deGAX)-platycodin D (PD) and deGAX-polygalacin D (PGD), respectively. The products were identified through LC/MS analysis by specifically hydrolyzing all glucose residues at C-3, and apiose and xylose residues at C-28 of platycoside. The hydrolytic activity of the crude enzyme obtained after the cultivation of the fungus using citrus pectin and corn steep solid as carbon and nitrogen sources, respectively, in culture medium was increased compared with those using other carbon and nitrogen sources. The crude enzyme from A. tubingensis was the most effective in producing deGAX platycoside at pH 5.0 and 60℃. The crude enzyme produced 0.32 mg/ml deGAX-PD and 0.34 mg/ml deGAX-PGD from 1 mg/ml PE and 1 mg/ml PGD3 (at pH 5.0 and 60℃) for 12 and 10 h, with productivities of 32.0 and 42.5 mg/l/h and molar yields of 62.1 and 59.6%, respectively. To the best of our knowledge, this is the first study to produce deGAX platycosides from glycosylated platycosides.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.5
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• pp.856-862
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• 1994

In salt-preserved foods of every kinds, it was examined the growth condition of halophilic bacteria that induced a change of colour, taste, nutritive substance, a production condition of enzyme and a character of crude enzyme. Used bacteria is H. halobium a kind of extremely halophilic bacteria, and the required of optimum culture needed a quite long time of crude enzyme production is 168 hours. Optimum pH is about 7-7.5, so the traditional food of such neutrality pH as soybean paste and soy sauce particularly come into trouble because the growth can flourish in neutrality or alkaliescence, and the crude enzyme also appeared that best activation between pH 6 and pH 8. The optimum temperature is about 37$^{\circ}C$, the optimum temperature of enzyme is about 40 $^{\circ}C$ and the temperature stability is settled for 15 minutes and it is completely inactivated at 10 minutes. In the influence of each metal ion, Fe++ and Mn++ a stimulated the growth of H.halobium and the activation of enzyme, Cu++ and Zn++ were identified that made the growth and the activation of enzyme inhibit.

• Korean Journal of Food Science and Technology
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• v.43 no.5
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• pp.570-576
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• 2011

The effect of nuruks and crude amylolytic enzyme on free amino acid and volatile components of brown rice vinegar prepared by static cultures was investigated. Five groups consisted of AV (100% nuruk without crude amylolytic enzyme), BV (75% nuruk; 25% crude amylolytic enzyme), CV (50% nuruk; 50% crude amylolytic enzyme), DV (25% nuruk; 75% crude amylolytic enzyme) and EV (100% crude amylolytic enzyme without nuruk). Free amino acid content in AV vinegar (132.06 mg%) was lower than the others (184.56-191.22 mg%). Acetic acid, 3-methyl butyl acetate, acetoin and isoamyl alcohol were major volatile components as analyzed using gas chromatography-mass spectrometry after headspace solid-phase microextraction. Acetic acid in AV and EV samples represented 67.56% and 55.53% of total GC peak area, respectively. E-nose provided different patterns in each case showing variation in sensory properties.

• Korean Journal of Pharmacognosy
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• v.35 no.4 s.139
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• pp.309-314
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• 2004

By treating crude enzyme extract from Aspergillus kawachii, the liquiritigenin content in the licorice (Glycyrrhizae Radix) was significantly increased. The liquiritigenin content reached its maximum level (45.7 mg/g licorice extract) after 60 min of incubation with the crude enzyme extract at $37^{\circ}C$, while the inactivated crude enzyme treated control contained trace amount (about 0.11 mg/g) of liquiritigenin. The enzyme-treated licorice extract inhibited more than 50% DPPH radical at 100 ppm and this was about two times higher activity compared to the enzyme-untreated control.

• Toxicological Research
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• v.22 no.1
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• pp.39-45
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• 2006

As the antioxidant and free radical scavenger, glutathione (GSH) participates in the preservation of cellular redox status and defense against reactive oxygen species and xenobiotics. Glutamate-cysteine ligase (GCL; also known as ${\gamma}$-glutamylcysteine synthetase, EC 6.3.2.2) is the rate limiting enzyme in GSH synthesis. In the present study, the accurate method for determination of GCL activity in crude liver extracts was developed by measuring both ${\gamma}$-glutamylcysteine and GSH from cysteine in the presence of glutamate, glycine and an ATP-generating system. We added glycine to promote the conversion of ${\gamma}$-glutamylcysteine to GSH, and to minimize the possibility of ${\gamma}$-glutamylcysteine metabolism to cysteine and oxoproline by ${\gamma}$-glutamylcyclotransferase. We established optimal conditions and substrate concentrations for the enzyme assay, and verified that inhibition of GCL by GSH did not interfere with this assay. Therefore, this assay of hepatic GCL under optimal conditions could provide a more accurate measurement of this enzyme activity in the crude liver extracts.