• Title/Summary/Keyword: enzyme production

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Production of Angiotensin-I Converting Enzyme Inhibitory Hydrolysates from Egg Albumen

  • Kim, H.S.;Ham, J.S.;Jeong, S.G.;Yoo, Y.M.;Chae, H.S.;Ahn, C.N.;Lee, J.M.
    • Asian-Australasian Journal of Animal Sciences
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    • 제16권9호
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    • pp.1369-1373
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    • 2003
  • ACE (Angiotensin-I converting enzyme) inhibitory peptides derived from foods are thought to suppress high blood pressure by inhibiting ACE. We tried to make efficient production of the ACE inhibitory hydrolysate from egg albumen. A hydrolysate digested by neutrase presented the highest ACE inhibitory activity ($IC_50\;value=256.35{\mu}g/ml$) and the proper proteolysis was occurred by 1.0% enzyme addition and 4 h incubation at $47^{\circ}C$. Antihypertensive effect of neutrase hydrolysate was investigated in spontaneously hypertensive rats (SHR, n=5). Systolic blood pressure (SBP) was decrease by 6.88% (-14.14 mmHg, p<0.05) at 3 h after oral administration of 300 mg/kg body weight, and by 13.33% (-27.72 mmHg, p<0.05) by emulsified hydrolysate. These results showed that it is very effective to utilize egg albumen as a protein source for the production of ACE inhibitory peptides. However, further studies are required to investigate the methods to increase recovery yield and the isolation of active peptide is necessary for determining its sequence responsible for ACE inhibitory activity.

Cellulase Production in the Digestive Organs of Reticulitermes speratus, a Native Termite from Milyang, Korea

  • Lee, Young-Min;Kim, Yoon-Hee;Cho, Moon-Jung;Shin, Keum;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • 제38권5호
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    • pp.421-428
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    • 2010
  • This study investigated on enzyme production in the digestive organs of the native termite (Reticulitermes speratus) in Milyang, Korea. Four types of major cellulases [EG (endo-1,4-${\beta}$-glucanase), BGL (${\beta}$-glucosidase), CBH (cellobiohydrolase) and BXL (${\beta}$-1,4-xylosidase)] were present in the digestive organs of the termite. The strong enzyme activity for BGL was found from the native termite, and also shown that the enzyme was distributed in the salivary gland, foregut, and hindgut. BXL, which breaks down hemicellulose near the amorphous region, was detected mainly from salivary gland, foregut, and midgut. However, CBH was distributed mainly in the hindgut. Meanwhile, EG which degrades cellulose, was found mainly in the hindgut and salivary glands. These facts indicate that celluases production patterns are differ from different sites compare to the same species found in Japan, suggesting that enzyme production in the digestive organs of termites is changed according to their habitats.

2단계 고정화 효소반응기를 활용한 Cyclodextrin의 연속생산 (Continuous Production of Cyclodextrin in Two-Stage Immobilized Enzyme Reactor Coupled with Ultrafiltration Recycle System)

  • 이용현;이상호;한일근
    • 한국미생물·생명공학회지
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    • 제19권2호
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    • pp.171-178
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    • 1991
  • The two-stage enzyme reactor, packed with cyclodextrin glucanotransferase (CGTase) immobilized on Amberite IRA 900, coupled with ultrafiltration membrane was investigated for continuous production of cyclodextrin (CD). 5% (w/v) of soluble starch was partially cyclized, in the 0.1 l first-stage immobilized enzyme reactor, up to CD conversion yield of 10% (w/w) at retention time of 0.56hr and 1.5 units of immobilized CGTase/1g of carrier. In the second stage main immobilized enzyme reactor capacity of 1.5 l, the maximum CD conversion yield of 39% (w/v) was achieved at retention time of 2.8hr and 0.47 unit of CGTase/1 g of carrier. Unreacted residual dextrin was fractionated with ultrafiltration membrane, and then, recycled into the second-stage main bioreactor to increase the CD conversion yield. The most suitable membrane size and the volume concentration ratio (concentrate: filterate) for recycling of unreacted residual dextrin were found to be 5K dalton and 4:6, respectively. CD conversion yield was increased about 3~4% upon co-immobilization of pulluanase along with CGTase. Spent Amberite IRA 900 can be reutilized consecutively more than 3 times for immobilization of CGTase after regeneration.

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Aspergillus niger에 대한 Invertase의 생성 및 특성 (Production and Properties of Invertase from Aspergillus niger)

  • Hong, Jung-Min;Lee, Kyung-Ah;Kim, Jinyull;Park, Inshik
    • 한국식품영양과학회지
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    • 제19권6호
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    • pp.577-582
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    • 1990
  • Aspergillus niger로 부터 invertase 생성의 최적조건과 생성된 효소의 특성을 조사하였다. 곰팡이는 탄소원으로 inulin과 sucrose를, 질소원으로 yeast extract를 사용했을 때 최대효소 생성을 얻을 수 있었다. 또한 사용한 배지의 pH를 4.5, 배양온도를 3$0^{\circ}C$로 유지했을 때 효소생성이 높았다. 효소 활성을 위한 최적조건은 pH 5.0 및 5$0^{\circ}C$였다. 효소는 pH 6.0에서 가장 안정했으며, 또한 5$0^{\circ}C$이하에서 안정하였다. 효소는 Hg++, Ag+ 및 Cu++ 이온의 첨가에 의하여 불활성화 되었다.

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효소 전처리가 음식물 쓰레기의 산발효에 미치는 영향 (Effect of Enzymatic Pretreatment on Acid Fermentation of Food Waste)

  • 김희준;김성홍;최영균
    • 한국환경보건학회지
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    • 제31권4호
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    • pp.294-300
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    • 2005
  • Food waste can be a valuable carbon source in biological nutrient removal (BNR) systems because of high C/N and C/P ratios. However, food waste should be pretreated to promote its hydrolysis rate because hydrolysis reaction would be a rate-limiting step. This study investigates the influence of the enzymatic pretreatment on acid fermentation of food waste. Solubilization of particulate matter in food waste by using commercial enzymes was examined. The acidification efficiency and the volatile fatty acids (VFAs) production potential of enzymatically pretreated food waste were also examined. The highest volatile suspended solids (VSS) reduction was obtained with an enzyme mixture ratio of 1:2:1 of carbohydrase:protease:lipase. An optimum enzyme dosage for solubilization of food waste was $0.1\%$(V/V) with the enzyme mixture ratio of 1:2:1. In the acid fermentation of enzymatically pretreated food waste, $0.1\%$(V/V) enzyme mixture dosage for pretreatment result in the maximum VFAs production and the best VFAs fraction in soluble COD(SCOD). The VFAs production at this addition level was 3.3 times higher than that of no-enzyme added fermenter. The dominant VFAs present was n-butyrate followed by acetate.

A New Approach to Produce Resveratrol by Enzymatic Bioconversion

  • Che, Jinxin;Shi, Junling;Gao, Zhenhong;Zhang, Yan
    • Journal of Microbiology and Biotechnology
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    • 제26권8호
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    • pp.1348-1357
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    • 2016
  • An enzymatic reaction system was developed and optimized for bioconversion of resveratrol from glucose. Liquid enzyme extracts were prepared from Alternaria sp. MG1, an endophytic fungus from grape, and used directly or after immobilization with sodium alginate. When the enzyme solution was used, efficient production of resveratrol was found within 120 min in a manner that was pH-, reaction time-, enzyme amount-, substrate type-, and substrate concentration-dependent. After the optimization experiments using the response surface methodology, the highest value of resveratrol production (224.40 μg/l) was found under the conditions of pH 6.84, 0.35 g/l glucose, 0.02 mg/l coenzyme A, and 0.02 mg/l ATP. Immobilized enzyme extracts could keep high production of resveratrol during recycling use for two to five times. The developed system indicated a potential approach to resveratrol biosynthesis independent of plants and fungal cell growth, and provided a possible way to produce resveratrol within 2 h, the shortest period needed for biosynthesis of resveratrol so far.

재래식 메주로부터 분리한 Mucor racemosus f. racemosus PDA 103이 생산하는 Fungal Protease 특성 (Characteristics of Fungal Protease Produced by Mucor racemosus f. racemosus from Korean Traditional Meju)

  • 임성일;유진영
    • 한국미생물·생명공학회지
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    • 제27권6호
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    • pp.466-470
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    • 1999
  • Protease production and its characteristics were investigated with Mucor racemosus f. racemosus PDA 103 which was isolated from Korean traditional meju. Optimum culture conditions of the strain for the production of the protease in basic medium[bean(Baektae):H2O=1:1(w/v)] were as follows: pH 6, 3$0^{\circ}C$ and 72hrs. Optimum pH and temperature for the enzyme activity of the protease produced by Mucor racemosus f. racemosus were pH 5 and 5$0^{\circ}C$, respectively. The enzyme was relatively stable a pH2.0~5.0 and at temperature below 4$0^{\circ}C$. Phenylmethane-sulfonyl fluoride and Ag+ inhibited the enzyme activity. This indicates that the enzyme is serine protease. Km value was 0.9$\times$10-4M and Vmax value was 5.93$\mu\textrm{g}$/min. This enzyme hydrolyzed casein more rapidly than bovine albumin.

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Serum Deprivation Enhances Apoptotic Cell Death by Increasing Mitochondrial Enzyme Activity

  • Moon, Eun-Yi
    • Biomolecules & Therapeutics
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    • 제16권1호
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    • pp.1-8
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    • 2008
  • Mitochondria are important sensor of apoptosis. $H_2O_2-induced$ cell death rate was enhanced by serum deprivation. In this study, we investigated whether serum deprivation using 0.5 or 3 % FBS induces apoptotic cell death through mitochondrial enzyme activation as compared to 10 % FBS. Apoptotic cell death was observed by chromosome condensation and the increase of sub-G0/G1 population. Serum deprivation reduced cell growth rate, which was confirmed by the decrease of S-phase population in cell cycle. Serum deprivation significantly increased caspase-9 activity and cytochrome c release from mitochondria into cytosol. Serum deprivation-induced mitochondrial changes were also indicated by the increase of ROS production and the activation of mitochondrial enzyme, succinate dehydrogenase. Mitochondrial enzyme activity increased by serum deprivation was reduced by the treatment with rotenone, mitochondrial electron transport inhibitor. In conclusion, serum deprivation induced mitochondrial apoptotic cell death through the elevation of mitochondrial changes such as ROS production, cytochrome c release and caspase-9 activation. It suggests that drug sensitivity could be enhanced by the increase of mitochondrial enzyme activity in serum-deprived condition.

Flammulina velutipes에 의한 Laccase의 생산과 효소적 특성 (Production and Enzymatic Properties of Laccase from Flammulina velutipes)

  • 이재성;서달선
    • 한국균학회지
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    • 제13권2호
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    • pp.111-114
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    • 1985
  • The production of lac case by the funguson various media was studied. The characteristics of the enzyme were also studied regarding to the optimum pH, stability, Km value, and inactivation. The maximum activity of laccase reached the 40 days of incubation and the barley straw extract appeared to be a strong inducer for laccase. The enzyme showed stability at wide range of pH with optimum pH of 6.6. Temperature stability of the enzyme was high. Laccase was not inactivated by the organic solvents used for the precipitation. The enzyme, how­ever, was completely inactivated by trichloroacetic acid and sodium azide.

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Bacillus sp. CW-1121이 생성하는 Alkaline Proteas의 생산 및 정제 (Production and Purification of Alkaline Protease from Bacillus sp. CW-1121)

  • 이우제;손규목;최청
    • 한국식품영양과학회지
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    • 제20권4호
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    • pp.388-394
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    • 1991
  • Alkaline protease producing bacteria were isolated from soil and identified as Bacillus sp. CW-1121. It was found that the production of alkaline protease reached to maximum in 5 day of fermentation at 4$0^{\circ}C$. The enzyme was purified by ammonium sulfate precipitation, gel filtration on Sephadex G-150 and DEAE-cellulose ion-exchange chromatography. The homogeneity of the purified enzyme was verified by polyacrylamide gel electrophoresis. The enzyme was purified 5.72 fold and yield of the enzyme purification was 16.71%. When the purified enzyme was applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated to be 55, 000.

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