• Food Science and Biotechnology
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• 제18권6호
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• pp.1519-1522
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• 2009

This study reports the use of different inducing agents (olive, soybean, and used frying oils) and culture mediums [synthetic medium (SM), whey protein, and corn steep liqueur (SL)] to optimize the production of lipase by Fusarium oxysporum. A relationship among the inoculum size, presence of a fat source, fungal growth, and lipase production was evident during the fermentation. The best results were achieved when the inoculum was grown in SM or SL and the fermentation was developed in SM with frying oil as the inducing agent. The maximum activity (about 15 U/mL) was obtained after a 72 hr cultivation.

• 한국미생물·생명공학회지
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• 제47권4호
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• pp.546-554
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• 2019

This study, for the first time, reports the functional expression of lipase B derived from the yeast Candida antarctica (CALB) in Corynebacterium strain using the Escherichia coli plasmid PK18. The CALB gene fragment encoding a 317-amino-acid protein was successfully obtained from the total RNA of C. antarctica. CALB was readily produced in the Corynebacterium strain without the use of induction methods described in previous studies. This demonstrated the extracellular production of CALB in the Corynebacterium strain. CALB produced in the Corynebacterium MB001 strain transformed with pEC-CALB recombinant plasmid exhibited maximum extracellular enzymatic activity and high substrate affinity. The optimal pH and temperature for the hydrolysis of 4-nitrophenyl laurate by CALB were 9.0 and 40℃, respectively. The enzyme was stable at pH 10.7 in the glycine-KOH buffer and functioned as an alkaline lipase. The CALB activity was inhibited in the presence of high concentration of Mg²⁺, which indicated that CALB is not a metalloenzyme. These properties are key for the industrial application of the enzyme.

• Asian-Australasian Journal of Animal Sciences
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• 제30권2호
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• pp.192-197
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• 2017

Objective: The study was conducted to evaluate the stability of commercial coated lipase (CT-LIP) in vitro. Methods: The capsules were tested under different conditions with a range of temperature, pH, dry heat treatment and steaming treatment, simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) in this work, respectively. Free lipase (uncoated lipase, UC-LIP) was the control group. Lipase relative activities measured in various treatments were used as a reference frame to characterize the stability. Results: The lipase activities were decreased with increasing temperatures (p<0.05), and there was a markedly decline (p<0.01) in lipase comparative activities of UC-LIP at $80^{\circ}C$ compared with CT-LIP group. Higher relative activities of lipase were observed in CT-LIP group compared with the free one under acidic ambient (pH 3 to 7) and an alkaline medium (pH 8 to 12). Residual lipase activities of CT-LIP group were increased (p<0.05) by 5.67% and 35.60% in dry heat and hydrothermal treatments, respectively. The lipase relative activity profile of CT-LIP was raised at first and dropped subsequently (p<0.05) compared with constantly reduced tendency of UC-LIP exposed to both SGF and SIF. Conclusion: The results suggest that the CT-LIP possesses relatively higher stability in comparison with the UC-LIP in vitro. The CT-LIP could retain the potential property to provide sustained release of lipase and thus improved its bioavailability in the gastrointestinal tract.

• 한국펄프종이공학회:학술대회논문집
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• 한국펄프종이공학회 2006년도 PAN PACIFIC CONFERENCE vol.1
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• pp.129-136
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• 2006

Although cleaner and cheaper deinking of ONP could be performed at the neutral or low alkaline condition excessive loss from froth-flotation is unavoidable and so reduction of alkali or caustic soda dosage sacrifices recycling yield. Now the new trade-off regarding alkali dosage versus flotation yield is urgently required in order to set the optimized neutral or low alkaline deinking process of ONP. Lipase from Thermomyces Lanuginosus has an effect on desizing and deacetylation reaction and it could be applied to the stock of pre flotation secondary stage in order to reduce the flotation reject without the sacrifice of optical properties of flotation accepts. Instead of inorganic base, lipase could be applied as a biochemical catalyst for the selective modification of valuable hydrophobic particles in deinking stock, for example cellulose fines and inorganic fillers covered by hydrophobic additives or contaminants. When the enzymatic hydrolysis of ester bond could be made on the surface of hydrophobic particulates, unwanted float of fine particles could be prevented. Now the enhancement of flotation selectivity or the modification of the hydrophobicity of deinking stock is expected to be promoted by the enzymatic pre treatment. And the reduction of recycling cost with the saves of raw material, recovered paper would be possible as a result.

• Journal of Microbiology and Biotechnology
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• 제25권12호
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• pp.2024-2033
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• 2015

A gene encoding lipolytic enzyme, lip7-3, was isolated from Bacillus sp. W130-35 isolated from a tidal mud flat. The gene encoded a protein of 215 amino acids with a signal peptide composed of 34 amino acid residues. Lip7-3 belonged to the family I.4 lipase and showed its maximal activity at pH 9.0 and 60℃. Its activity increased in the presence of 30% methanol and, remarkably, increased as well to 154.6% in the presence of Ca²⁺. Lip7-3 preferred p-nitrophenyl octanoate (C8) as a substrate and exhibited broad specificity for short- to long- chain fatty acid esters. Additionally, Lip7-3 showed a low degree of enantioselectivity for an S-enantiomer (e.g., (S)-methyl-3-hydroxy-2-methylpropionate). It efficiently hydrolyzed glyceryl tributyrate, but did not hydrolyze glyceryl trioleate, fish oil, or olive oil. Its substrate specificity and activation by the solvent might offer a merit to the biotechnological enzyme applications like transesterification in the production of biodiesel.

• Journal of Ginseng Research
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• 제5권1호
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• pp.49-55
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• 1981

The effects of total, protopanaxadiol-and protopanaxatriol-saponins on the in vitro activities of several enzymes in rat serum were observed Alkaline phosphatase activity was increased 61 % by total saponin and 46% by protopanaxatriol-saponin, compared to control group. While SCOT activity was slightly decreased by total saponin and protopanaxatriol- saponin, it was slightly increased by Protopanaxadiol-saponin And while SCPT activity was slightly decreased by total saponin, it was increased by protopanaxadiol-saponin and protopanaxatriol-saponin. Creatine phosphokinase activity had a tendency to be increased by protopanaxatriol-saponin. Lactate dehydrogenase activities were increased in three saponin treated groups, but those were nonignificant. Compared to the control group, lipase activity was increased by all saponin samples. It was increased 157% by total saponin The increase in lipase activity by total saponin corresponded with the decrease in serum t total lipid by total saponin .

• 한국환경과학회지
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• 제28권5호
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• pp.475-483
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• 2019

The purpose this study was to investigate the influences of 5% turmeric (Curcuma longa L.) supplementation on enzyme activities such as aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), lactate dehydrogenase (LDH), amylase, lipase and catalase in serum of dyslipidemic rats. Sprague-Dawley (SD) rats (24 male) were divided into four groups, namely the ND group (normal-nondyslipidemic diet), NT group (normal-nondyslipidemic diet+5% turmeric), DD group (control-dyslipidemic diet), and DT groups (dyslipidemic diet+5% turmeric). Serum concentrations of blood urea nitrogen (BUN), creatinine and uric acid were significantly decreased (p<0.05) by turmeric supplementation diet. The activities of AST, ALT, ALP, LDH, amylase and lipase in sera of turmeric diet group were significantly decreased (p<0.05). The catalase activity in serum of turmeric supplementation group was significantly increased than dyslipidemic diet (p<0.05). In vivo experiment with dyslipidemic rats showed that ingestion of turmeric were effective in kidney and hepatic functional enzyme activities. Which suggests that turmeric material could be used for further studies as a potential source for nutraceutical foods.

• 한국응용과학기술학회지
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• 제39권6호
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• pp.760-768
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• 2022

본 연구의 목적은 5% 녹두(Phaseolus aureus L.)의 급여가 고지혈증 유발 Sprague-Dawley(SD)계 흰쥐의 혈청 blood urea nitrogen(BUN), creatinine 및 요산(uric acid)의 농도와 aspartate aminotransferase(AST), alanine aminotransferase(ALT), alkaline phosphatase(ALP), lactate dehydrogenase(LDH), amylase, lipase 및 catalase 활성에 미치는 영향을 규명하고자 시행하였다. 연구결과 녹두는 고지혈증으로 유발된 흰쥐의 혈청 BUN, creatinine, 요산 농도 및 AST, ALT, ALP, LDH, amylase, lipase의 활성 감소와 catalase 활성을 증가시키는 것으로 나타났다. 따라서 녹두는 신장과 간 등의 기능 개선과 예방에 효과적일 것으로 판단되어 기능성 소재로서의 이용 가능성이 있을 것으로 기대된다.

• 한국미생물·생명공학회지
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• 제33권1호
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• pp.29-34
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• 2005

새만금 갯벌로부터 리파제를 생산하는 균주(S3)를 분리하였다. 생리적, 발효적 특성 및 계통분류학적 특성을 통해서 이 분리균이 Psychrobacter속에 속하는 것으로 판명되어서 Psychrobacter sp. S3로 명명하였다 이 균의 온도에 따른 배양특성을 구한 결과, $30^{\circ}C$에서 생장속도가 가장 빨랐으나, 리파제 효소의 활성은 $20^{\circ}C$에서 가장 높았다. S3리파제의 온도에 따른 p-nitrophenyl caproate 분해활성을 측정한 결과, 최적 온도가 $30^{\circ}C$로 판명되었으며 $10^{\circ}C$에서도 최고활성의 $80\%$ 이상의 활성을 유지하였다. 또한, $10-30^{\circ}C$범위에서의 효소활성에너지가 1.5 kcal/mol로 매우 낮게 계산되었다. 이것을 통해 S3 리파제가 전형적인 저온성 효소임이 확인되었다. 이 효소는 최적 pH가 $9.0\~9.5$인 알칼리성 효소로 확인되었다. 여러 길이의 트리글리세리드 기질을 분해할 수 있으며 그 중에서 $C_4,\;C_{14},\; C_{16}$기질을 가장 빠르게 분해하였다. S3리파제를 트리뷰티린-아가로스 젤에 가하여 온도별로 반응시킨 결과, $30^{\circ}C$와 $40^{\circ}C$에서 반응이 빠르게 진행되었으나, $4^{\circ}C$에서도 분해가 진행되었다.

• 대한수의학회지
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• 제48권4호
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• pp.451-455
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• 2008

Body weights and blood biochemical values in chickens infected with reticuloendotheliosis virus (REV)-HI, a Korean isolate, were studied. REV-HI causes severe body weight depression in chickens inoculated but not in chicken contact-infected. Body weights of infected chickens in 3, 4, and 5 weeks after infection were 78%, 76% and 65% of those of control respectively. Blood glucose levels in REVinfected chickens were extremely high compared with those in control (226 $\geq$ 21 vs. 814 $\geq$91.3 mg/dl in week 2) during the experiment period. Triglyceride levels in REV-infected chickens were significantly higher in week 2 and 3, whereas in week 4, REV-infected chickens showed significantly lower levels than the control. Blood lipase, amylase and alkaline phosphatase levels of REV-infected chickens in week 2 were significantly higher, whereas cholesterol, magnesium and calcium values in week 4 were significantly lower than the control. Other blood biochemical values such as alkaline aminotransferase, aspartate aminotransferase, and $\gamma$-glutamyltransferase were nonsignificantly different from the control. These above results suggest that weight depression by REV may be related with increase of blood glucose, which indicated that REV-infected chickens could not use blood glucose as energy source.