• Journal of the Korean Society of Food Science and Nutrition
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• v.36 no.6
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• pp.766-772
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• 2007

The enzymatic hydrolysate of skipjack tuna cooking drip with good functionality was prepared by incubation with Alcalase for 30 min. For the preparation of functional seasoning sauce with enzymatic hydrolysate (SSE), the additives, such as concentrated enzymatic hydrolysate (100 mL), yeast extract powder (0.7 g), lactose (0.4 mL), liquid smoke (0.3 g) and sea tangle powder (1.4 g), were added to the enzymatic hydrolysate and boiled before filtration. The proximate composition of SSE was 11.8% for crude protein, 5.77 for pH and 11.9% for salinity. The SSE was higher in the crude protein, while lower in the salinity than commercial seasoning sauce. ACE inhibitory activity ($IC_{50}$) and antioxidative activity (PF) of SSE were 6.2 mg/mL and 1.14, respectively, which were superior to those (9.9 mg/mL in IC50 and 0.91 in PF) of commercial seasoning sauce. The free amino acid content (1,905.2 mg/100 mL) and taste value (58.65) of SSE were higher than in those (712.7 mg/100 mL and 34.30, respectively) of commercial sauce. Total amino acid content of SSE (10,965 mg/100 mL) was higher than that (4,818 mg/100 mL) of commercial sauce. The major amino acids of SSE were glutamic acid (12.2%), proline (11.0%), histidine (10.7%) and glycine (9.9%). The results suggested that SSE could be commercially sold.

• Korean Journal of Microbiology
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• v.48 no.2
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• pp.73-78
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• 2012

We previously reported that the truncated Cel44C-$Man26A_{P558}$ ${\beta}$-glycosyl hydrolase protein exhibits multifunctional activities, including cellulase, xylanase, and lichenase. DNA shuffling of the truncated Cel44C-$Man26A_{P558}$ enzyme was performed to enhance the enzymatic activity of the multifunctional ${\beta}$-glycosyl hydrolase. Two mutant enzymes, M2Cel44C-$Man26A_{P558}$ that carries one mutation (P438A) and M21Cel44C-$Man26A_{P558}$ that carries two mutations (A273T and P438A) were obtained. The enzymatic activity of the M21Cel44C-$Man26A_{P558}$ double mutant was lower than enzymatic activity of the single mutant (M2Cel44C-$Man26A_{P558}$). However, both mutants displayed the enhancements in their enzyme activities that were ${\approx}1.3$- to 2.2-fold higher than the original enzymatic activity in Cel44C-$Man26A_{P558}$. In particular, the mutant M2Cel44C-$Man26A_{P558}$ exhibited an approximate 1.5- to 2.2-fold increase in the cellulase, xylanase, and lichenase activities in comparison with the control (Cel44C-$Man26A_{P558}$). The optimum cellulase, linchenase, and xylanase activities of ${\beta}$-glycosyl hydrolase were observed at pH 7.0, pH 7.0 and pH 6.0, respectively. These results, therefore, suggest that the amino acid residue Ala438 plays important roles in the enhancement of the activity of multifunctional ${\beta}$-glycosyl hydrolase.

• Journal of Microbiology
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• v.45 no.6
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• pp.485-491
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• 2007

The effects of biological pretreatment on the Japanese red pine Pinus densiflora, was evaluated after exposure to three white rot fungi Ceriporia lacerata, Stereum hirsutum, and Polyporus brumalis. Change in chemical composition, structural modification, and their susceptibility to enzymatic saccharification in the degraded wood were analyzed. Of the three white rot fungi tested, S. hirsutum selectively degraded the lignin of this sortwood rather than the holocellulose component. After eight weeks of pretreatment with S. hirsutum, total weight loss was 10.7%, while lignin loss was the highest at 14.52% among the tested samples. However, holocellulose loss was lower at 7.81 % compared to those of C. lacerata and P. brumalis. Extracelluar enzymes from S. hirsutum showed higher activity of ligninase and lower activity of cellulase than those from other white rot fungi. Thus, total weight loss and changes in chemical composition of the Japanese red pine was well correlated with the enzyme activities related with lignin- and cellulose degradation in these fungi. Based on the data obtained from analysis of physical characterization of degraded wood by X-ray Diffractometry (XRD) and pore size distribution, S. hirsutum was considered as an effective potential fungus for biological pretreatment. In particular, the increase of available pore size of over 120 nm in pretreated wood powder with S. hirsutum made enzymes accessible for further enzymatic saccharification. When Japanese red pine chips treated with S. hirsutum were enzymatically saccharified using commercial enzymes (Cellulclast 1.5 L and Novozyme 188), sugar yield was greatly increased (21.01 %) compared to non-pre treated control samples, indicating that white rot fungus S. hirsutum provides an effective process in increasing sugar yield from woody biomass.

• Korean Journal of Food Science and Technology
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• v.29 no.2
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• pp.355-361
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• 1997

This study was carried out to investigate the acute cutaneous enzymatic antioxidant activity of green tea extracts (GTE) on hairless mice skin after a signal exposure to ultraviolet B radiation. GTE has been in corporated at concentration of 5, 25, 50 and $100\;{\mu}g$ into hairless mice skin. Under exposure conditions of $1.0\;joule/cm^{2}$, impairment of cutaneous enzymatic activity was observed. Catalase and glutathione reductase were significantly influenced in dose-dependent manner by GTE, however glutathione peroxidase and superoxide dismutase were not affected. To measure inhibition effect of the GTE on lipoxygenase. $50\;{\mu}g$ GTE extract was added in vitro to arachidonis acid. GTE showed higher inhibition effect on 5-hydroxyeicosatetraenoic acid (HETE) and 8-HETE than metalolic products of 12- or 15-HETE. The addition of 5, 25, 50 and $100\;{\mu}g$ GTE inhibited the metabolite formation of 5-HETE by 32, 52, 62 and 80%, respectively, and the metabolite formation of 8-HETE by 36, 47, 70 and 84%, respectively.

• Journal of Microbiology and Biotechnology
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• v.27 no.6
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• pp.1120-1127
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• 2017

Marasmius scorodonius secretes an extracellular laccase in potato dextrose broth, and this enzyme was purified up to 206-fold using $(NH_4)_2SO_4$ precipitation and a Hi-trap Q Sepharose column. The molecular mass of the purified laccase was estimated to be ~67 kDa by SDS-PAGE. The UV/vis spectrum of the enzyme was nontypical for laccases, and metal content analysis revealed that the enzyme contains 1 mole of Fe and Zn and 2 moles of Cu per mole of protein. The optimal pH for the enzymatic activity was 3.4, 4.0, and 4.6 with 2,2'-azino-bis(3-ethylbenzothazoline-6-sulfonate) (ABTS), guaiacol, and 2,6-dimethoxy phenol as the substrate, respectively. The optimal temperature of the enzyme was $75^{\circ}C$ with ABTS as the substrate. The enzyme was stable in the presence of some metal ions such as $Ca^{2+}$, $Cu^{2+}$, $Ni^{2+}$, $Mg^{2+}$, $Mn^{2+}$, $Ba^{2+}$, $Co^{2+}$, and $Zn^{2+}$ at a low concentration (1 mM), whereas $Fe^{2+}$ completely inhibited the enzymatic activity. The enzymatic reaction was strongly inhibited by metal chelators and thiol compounds except for EDTA. This enzyme directly decolorized Congo red, Malachite green, Crystal violet, and Methylene green dyes at various decolorization rates of 63-90%. In the presence of 1-hydroxybenzotriazole as a redox mediator, the decolorization of Reactive orange 16 and Remazol brilliant blue R was also achieved.

• Preventive Nutrition and Food Science
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• v.13 no.4
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• pp.313-320
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• 2008

Efficiency of a far-infrared radiation (FIR) dryer for drying of citrus by-products (CBPs) was evaluated through their antioxidant activities. The CBPs dried through FIR were enzymatically digested by six carbohydrases (AMG, Celluclast, Pectinase, Termamyl, Ultraflo and Viscozyme) to prepare digests for evaluation of the activities. The total polyphenolic and total flavonoid contents of the digests were determined by colorimetric assays. The AMG digest was selected for the further experiments. The antioxidant potential of the digests were evaluated by DPPH, superoxide, hydroxyl and alkyl radical scavenging activities, $H_2O_2$ scavenging activity, metal chelating, lipid peroxidation inhibition and the reduction of DNA damage. The AMG digest from CBPs dried through FIR at $50^{\circ}C$ showed strong antioxidant activities in DPPH, superoxide, hydrogen peroxide, alkyl and metal chelating assays while all the digests showed strong lipid peroxidation activities. Further, enzymatic digests showed remarkable inhibitory activities against $H_2O_2$-induced DNA damage. Hence, the data obtained using different in vitro models clearly established the antioxidant potential of enzymatic digests from CBPs dried through FIR. Furthermore, they can be used as a source of natural antioxidants; hence, far-infrared radiation drying is a viable method for transforming wet CBPs into a dried form without destroying the bioactive components.

• KSBB Journal
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• v.18 no.5
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• pp.363-370
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• 2003

A filamentous fungus, strain FM04 producing amylase was isolated from rotten yam peels and potatoes. The favorable conditions of cultivation factors such as, temperature, pH, and agitation speed of strain FM04 were 28∼30$^{\circ}C$, 5.0∼6.0, and 100 rpm, respectively. Starch was the best carbon source in the amylase production. Therefore, food wastes containing lots of starch were employed as the carbon source of the cultivation for the economical amylase production. 5.2 U/ml of amylase was obtained In the cultivation using 1 % (w/v) of food wastes. The amylase showed the highest activity at enzyme reaction conditions of 60$^{\circ}C$ and pH 4.5 and showed 90% of residual activity after the reaction at 50$^{\circ}C$ for 2 days. In the enzymatic hydrolysis reaction using 20% (w/v) of food wastes and 2.5 U/ml of amylase, 72.6 g/l of reducing sugar was obtained at the reaction condition of 50$^{\circ}C$, pH 4.5 for 2 days.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1995.04a
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• pp.107-107
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• 1995

The purpose of this study was to observe the effects of the polysaccharide(G009) obtained from liquid cultured Ganoderma lucidum IY009 on the lipidperoxidation in rat liver microsome. It is well known that the polysaccharide of G. lucidum have the hepatoprotective activity, antitumor activity etc., which was thought to have the relationship to anti-lipidperoxidation. In order to the estimate the effects of anti-lipidperoxidation of the polysaccharide obtained from G. lucidum IY009, enzymatic and nonenzymatic reaction were performed, in vitro, in rat liver microsome. In enzymatic lipid peroxidation reaction by ADP/FeCl$_3$/NADPH and $CCl_4$/NADPH, G009(1mg/ml) inhibited 77.4%, 39.4%, respectively, and the nonenzymatic reaction strongly exhibited 97.4% inhibition. And also, in enzymatic and nonenzymatic inducers treated with G009, the formation of MDA was progressively greater decreased by raising G009 concentration. These results suggest that anti-lipidperoxidation by G009 treatment may be play an important part in liver protection action.

• Korean Journal of Food Science and Technology
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• v.4 no.4
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• pp.300-308
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• 1972

For the purpose of utilizing agricultural waste products for animal feeds, chemical analysis of some important agricultural wastes in Korea and enzymatic hydrolysis of rice hull were undertaken and summarized as follows: 1) Rice hull and straws of rice, barley and wheat were analyzed for their proximate principles and carbohydrate composition. 2) A strain of Aspergillus niger was selected as having the highest productivity of rice hull decomposing activity among many species of molds. The optimum conditions for the culture on washed wheat bran were. 3 days of culture period, 55% moisture content and neutral pH and one hour was proper for the extraction of enzymes. 3) The extent of hydrolysis of xylan and rice hull by a crude enzyme preparation from this strain was 63% and 7%, respectively, and the optimum pH for its activity was 4.0 and 4.5, respectively. 4) Enzymatic hydrolysis of rice hull was generally suppressed by gamma-ray irradiation ($0.5{\sim}5\;Mrad$, in dry state), but the effect was less by irradiation in wet state.

• Natural Product Sciences
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• v.16 no.1
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• pp.1-5
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• 2010

$\beta$-Glucuronidases (E.C. 3.2.1.31) from Escherichia coli, Helix pomatia, and bovine liver activity have been investigated on 7-O-glucuronides (baicalin, wogonoside, and luteolin-7-O-glucuronide) and 3-O-glucuronides (quercetin-3-O-glucuronide and kaempferol-3-O-glucuronide). Bovine liver enzyme was not active on any of these substrates. E. coli and H. pomatia enzymes were active on 7-O-glucuronides, however, 3-O-glucuronides were resistant to $\beta$-glucuronidase hydrolysis. These results suggest that glucuronic acid at 7-position is more susceptible to E. coli and H. pomatia $\beta$-glucuronidases than that at 3-position. In addition, the subtle difference of aglycone structure on 7-O-glucuronides affected the preference of enzyme. E. coli enzyme was favorable for the hydrolysis of baicalin, however, H. pomatia enzyme was found to be efficient for the hydrolysis of wogonoside. Both enzymes showed the similar hydrolytic activity towards luteolin-7-O-glucuronide. When the Scutellaria baicalensis crude extract was subjected to enzymatic hydrolysis, baicalin and wogonoside were successfully converted to their aglycone counterparts with H. pomatia at 50 mM sodium bicarbonate buffer pH 4.0. Accordingly, the enzymatic transformation of glycosides may be quite useful in preparing aglycones under mild conditions.