• 제목/요약/키워드: enzyme solution

검색결과 698건 처리시간 0.023초

흰쥐의 간(肝) 조직(組織)에서 녹용(鹿茸) 약침(藥針) 제제(製劑)의 항산화작용(抗酸化作用)에 관(關)한 연구(硏究) (Effects of Cervus elaphus for herb-acupuncture solution on Antioxidation in Rat‘s liver)

  • 윤철호;정지천;신억섭
    • 대한한의학회지
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    • 제17권2호
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    • pp.191-202
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    • 1996
  • Cervus elaphus for herb-acupuncture solution(CEHAS) was tested for the effects of free radical generating enzyme and lipid peroxidation in rat's liver. In vitro, levels of lipid peroxide in tissues of liver were proportionally decreased to concentration of CEHAS. They were much more decreased. when lipid peroxidation was induced with ferrous iron $(Fe^{-2})$. Also, enzyme activities of xanthine oxidase were decreased. The ratio of type conversion of xanthine oxidase was lowered, too. But, here was not special changes on enzyme activities of aldehyde oxidase. These results suggest that CEHAS decrease the activities of free radical generating enzymes such as xanthine oxidase which form lipid peroxide.

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녹용(鹿茸) 약침(藥針) 제제(製劑)가 흰쥐 신장(腎臟) 조직(組織)의 항산화(抗酸化) 작용(作用)에 미치는 영향(影響) (Effects of Cervus elaphus for herb-acupuncture solution on Antioxidation in Rat's kidney)

  • 윤철호;정지천;신억섭
    • 한국한의학연구원논문집
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    • 제2권1호
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    • pp.192-204
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    • 1996
  • Cervus elaphus for herb-acupuncture solution (CEHAS) was tested for the effects of free radical generating enzyme and lipid peroxidation in rat's kidney. In vitro, levels of lipid peroxide in tissues of kidney were proportionally decreased to concentration of extracts prepared from CEHAS. They were much more decreased, when lipid peroxidation was induced with ferrous iron (FeII). Also, enzyme activities of xinthine oxidase were decreased. The ratio of type conversion of xanthine oxidase was lowered, two. But, it was not seen changes on enzyme activities of aldehyde oxidase. These results suggest that CEHAS decrease the activities of free radical generating enzymes such as xanthine oxidase which form lipid peroxide.

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완두와 보리의 엽내세포 원형질체 분이 및 융합 (The Isolation and Fusion of Pea and Barley Mesophyll Protoplasts)

  • 이광웅
    • Journal of Plant Biology
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    • 제23권2호
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    • pp.49-54
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    • 1980
  • The optimal conditions for the protoplast isolation from the leaves of pea (Pisum sativum L. cv. Sparkle) and barley (Hordeum vulgare L. cv. Baecdong) were determined in order to achieve a somatic hybridization between two species. It was revealed that the use of 0.5M sorbitol as an osmoticum was appropriate for pea. The yield of intact protoplasts was the highest (40%) when pea leaves were incubated in the enzyme solution for 4 hours. In case of barley, the optimal concentrations of cellulase, pectinase and mannitol as the enzyme solution were 2%, 1% and 0.35M, respectively. And the yield of barley protoplasts was the highest(87%) when leaves were incubated in this enzyme solution for 3.5 hours. A fusion of protoplasts from pea and barley was induced by PEG treatment enriched with calcium salts within 60 minutes.

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Protease (Subtilisin Carlsberg) 가 혈액 단백질 오구의 제거에 미치는 영향(II) -헤모글로빈 오구포의 세척성- (Effect of Pretense (Subtilisin Carlsberg) on the Removal of Blood Protein Soil (II) -The Detergency of Hemoglobin from Cotton Fabics-)

  • 이정숙;김성연
    • 한국의류학회지
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    • 제20권4호
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    • pp.655-666
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    • 1996
  • The effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The relation between the renloval and the hydrolysis of hemoglobin by subtilisin Carlsberg was discussed. The soiled babric was prepared by spotting of hemoglobin solution evenly on the cotton fabric and was denatured by steaming. The soiled fabric was washed by using Terg-0-Tometer at various conditions. The removal efficiency was evaluated by analysis of protein on the fabrics before and after washing by means of copper-Folin method. 1. The removal of hemoglobin was increased in proportion to increasing of the enzyme concentration up to a certain point, but it began to decrease above the point. 2. The hemoglobin was removed effectively by adding of subtilisin Carlsberg, and more effectively removed by adding of AOS in the enzyme solution. 3. The removal of hemoglobin deviated from the first order reaction in detergency. 4. The renloval of hemoglobin was highest at $50^{\circ}C$ in detergency, Even at low temperature the removal efficiency of enzyme was relatively higher compared with the hydrolysis of hemoglobin by the enzyme. However the removal of hemoglobin was apparently decreased with the increase of temperature over $60^{\circ}C$. 5. The removal of hemoglobin was relatively high at pH 7.0~8.0 and increased continuously with the increase of pH in detergency 6. In detergency, the removal mechanism of hemoglobin by subtilisin Carlsberg could be explained as follows: Fisrt of all, the enzyme hydrolyzed hemoglobin substrates partially by forming E-S complex at the surface of hemoglobin on the cotton fiber, and decomposed cooperative binding of hemoglobin. Subsequently, the fragments of hemoglobin were easily removed by washing. According as the enzyme penetrated to inner part of hemoglobin gradually, the hemoglobin on the cotton fiber was effectively removed by the repetition of these process. The removal of hemoglobin was more effectively increased by adding both the enzyme and AOS in the washing solution. Therefore, it was regarded that AOS molecules were adsorbed at the hydrophobic surface of denatured hemoglobin, subsequently, decomposed more effectively cooperative binding of hemoglobin, and the fragments of hemoglobin were removed more efficiently by means of the interfacial reaction of AOS.

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대두 가수분해물의 혈압 강하 효과 및 기능성 (Functionality and Inhibitory Effect of Soybean Hydrolysate on Angiotensin Converting Enzyme)

  • 서형주;김윤숙
    • 한국식품영양학회지
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    • 제9권2호
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    • pp.167-175
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    • 1996
  • This studies were conducted to select optimal enzyme that produced hydrolysate from soybean, and to evaluated functionality of hydrolysate. Soybean powder was suspended with water and hydrolyzed by seven commercial proteases. Hydrolysate produced with protease from Bacillus subtilis showed the highest inhibition effect on the activity of angiotension converting enzyme(ACE), and the condition of enzymatic hydrolysis was 5cA substrate concentration, 0. l% enzyme concentration, 4 hour hydrolysis time. Under above optimum condition, soybean was hydrolyzed with protease from Bacillus subtilis yielding a DH (degree of hydrolysis) of about 49%. Hyrophobicity of hydrolysate was not correlated with the inhibition effect on ACE activity. The functionality of hydrolysate was significantly influenced by pH. Solubility of hydrolysate at alkali solution was greater than that at acidic solution.

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소염효소제(消炎酵素劑)의 약제학적(藥劑學的) 연구(硏究) (Pharmaceutical Studies on Anti-inflammatory Enzyme Preparations)

  • 이강춘;양중익;민신홍;이상의;김용배
    • Journal of Pharmaceutical Investigation
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    • 제8권1호
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    • pp.27-36
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    • 1978
  • Spherical granules of anti-inflammatory enzyme were prepared by mixer granulation and the recovery rate of enzyme activity by processing was compared with tablet ones. In the enteric granule coating .processing, the effect of the amount of coating solution and the conentration of fatty alcohol on disintegration and stabilities on the accelerated conditions were also studied. Being prepared in non-pressure and non-aqueous condition, spherical granules of enzyme made better recovery of enzme activity than tablet ones by 10 times. Combined processing of both mixer granulation and enteric granule film coating provided the noble enteric coated granules, in the sense of disintegration and stabilities, was obtained from using 0.125% fatty alcohol in coating solution.

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遊離시간 , 酵素處理 및 2,4-D 농도가 재래 유자(Citrus junos)의 캘러스由來 原形質體 遊離 및 培養에 미치는 영향 (Effect of Incubation Time, Concentration of Enzyme, and 2,4-D on Isolation and Callus Formation of Protoplast from Callus of Citrus junos)

  • 오성도;김영숙
    • 식물조직배양학회지
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    • 제25권5호
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    • pp.335-339
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    • 1998
  • 미숙배주조직 유래의 배발생캘러스를 이용하여 원형질체의 유리 및 배양에 미치는 요인을 조사하였다. 배발생캘러스로부터 원형질체를 유리시키는데 적당한 배양시간은 16시간이었고, 건전한 원형질체를 유리하는데 적당한 효소용액의 농도는 0.7M $\textrm{BH}_{3}$ 용액과 cellulase 1.0%, macerozyme 1.0%, pctolyase 0.2%가 혼합된 효소용액을 동량으로 조합하였을 때가 가장 효과적이었다. 유리된 원형질체는 MT기본배지에 0.1 mg/L 2,4-D를 첨가한 배지로 배양하면 캘러스 형성이 양호하였다. 유도된 캘러스는 고체배지에 계대배양하고 있으나 생육이 징약한 상태이다. 본 실험결과 배발생캘러스유래의 원형질체와 엽육세포유래의 원형질체 융합에 의한 배양도 가능할 것으로 생각되었다.

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유기용매 첨가에 따른 Polypyrrole-Glucose Oxidase 효소전극의 효소고정화 향상 I. 자외선 분광분석 (Improvement on Enzyme Immobilization in Polypyrrole-Glucose Oxidase Enzyme Electrode using Organic Solvent Additive I. Ultraviolet Spectroscopic Analyses)

  • 김현철;구할본
    • 한국전기전자재료학회논문지
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    • 제15권7호
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    • pp.615-620
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    • 2002
  • In the case of immobilizing of glucose oxidase into polypyrrole (PPy) using electrosynthesis, the glucose oxidise (GOx) forms a coordinate bond with the polymers backbone. However, because of intrinsic insulation and net-chain of the enzyme, the charge transfer and mass transport are obstructed during the film growth. Therefore, the film growth is dull. We synthesized enzyme electrodes by electropolymerization added some organic solvent, such as ethanol and tetrahydrofuran (THF). The formative seeds of film growth was delayed by adding ethanol. The delay was induced by radical transfer between ethanol and pyrrole monomer. The radical transfer reactions shared the contribution of dopants between electrolyte anion and GOx polyanion. This led to increase amount of immobilized the enzyme in PPy. For the UV absorption spectra of synthetic solution before synthesis and after, in the case of ethanol added, the optical density was slightly decreased for the GOx peaks. It suggests amount of GOx in the solution was decreased and amount of GOx in the film was increased.

A Spontaneous Growth of a Diaphorase Enzyme Layer over a Gold Electrode for the Catalytic Reduction of $NAD^+$

  • 김소형;윤세옥;강찬
    • Bulletin of the Korean Chemical Society
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    • 제22권11호
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    • pp.1192-1196
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    • 2001
  • A diaphorase enzyme electrode for the catalytic reduction of NAD+ , the oxidized form of nicotinamide adenine dinucleotide, has been prepared. The enzyme layer grew spontaneously over an aminoethanethiol self assembled monolayer on a go ld plate electrode. The growth was accomplished by simply dipping the electrode covered by the aminoethanethiol monolayer into a solution containing both glutaraldehyde and diaphorase. We suggested that the glutaraldehyde as a cross-linking reagent was attached to the amino groups of the aminoethanethiol monolayer and the diaphorase enzyme molecules were bound to free aldehyde groups of the glutaraldehyde. Further attachments of the enzyme molecules over the bound enzyme molecules continued with the bridging of the glutaraldehyde. In frequency measurements with a quartz crystal microbalance, the frequency decrease was much more than it was for that of the enzyme monolayer formation, and an enzyme layer thicker than a monolayer was formed. The modified electrode was employed to reduce NAD+ , using diffusional methyl viologen as an electron transfer mediator. The NAD+ was electrocatalytically reduced, and the catalytic current was almost equivalent to that with the multilayered electrode of ten enzyme layers.

수송용 바이오 부탄올 생산을 위한 미강발효의 최적화 (Fermentation of rice bran and defatted rice bran for butanol production using Clostridium beijerinckii NCIMB 8052)

  • 이지은;서은종;박기문;진용수
    • 한국신재생에너지학회:학술대회논문집
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    • 한국신재생에너지학회 2008년도 춘계학술대회 논문집
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    • pp.235-238
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    • 2008
  • We examined butanol fermentation by Clostridium beijerinckii NCIMB 8052 using various hydrolyzates obtained from rice bran which is one of the most abundant agricultural by-products in Korea and Japan. In order to increase the amount of fermentable sugars in the hydrolyzates of rice bran, various hydrolysis procedures were applied. Total eight different hydrolyzates were prepared using rice bran (RB) and defatted rice bran (DRB) with enzyme or acid treatment and both. Each hydrolyzate was evaluated in terms of total sugar concentration and butanol production after fermentation by C. beijerinckii NCIMB 8052. Acid treatment yielded more sugar than enzyme treatment and combined treatment with enzyme and acid yielded even more sugars as compared to single treatment with enzyme or acid. As a result, the highest sugar concentration (33 g/L) was observed from the hydrolyzate from DRB (100 g/L) with combined treatment using enzyme and acid. Prior to perform fermentation of the hydrolyzates, we examined the effect of P2 solution containing yeast extract, buffer, minerals, and vitamins on production of butanol during the fermentation. Fermentation of the hydrolyzates with or without additionof P2 was performed using C. beijerinckii NCIMB 8052 in a 1 L anaerobic bioreactor. Although the hydrolyzates RB were able to support growth and butanol production, addition of P2 solution into the hydrolyzates significantly improved cell growth and butanol production. Highest butanol production (12.24 g/L) was observed from the hydrolyzate of DRB with acid and enzyme treatment after supplementation of P2 solution.

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