• Title/Summary/Keyword: enzymes

검색결과 6,187건 처리시간 0.037초

Biochemical Changes in Sugars and Cell Wall Degrading Enzymes during Ripening of Banana

  • Lee, Min-Kyung;Kim, Mi-Jeong;Park, Inshik
    • Preventive Nutrition and Food Science
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    • 제9권1호
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    • pp.92-94
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    • 2004
  • Changes in reducing sugar and cell wall degrading enzymes during ripening of banana for 10 days were investigated. The amount of reducing sugar in bananas increased during storage at room temperature during the first 7 days, and decreased thereafter. However, starch content in banana decreased during ripening, and invertase and cell wall degrading enzymes such as cellulase, polygalacturonase and xylanase were most active after bananas were stored for 7 days at room temperature. When the bananas were stored at 4$^{\circ}C$, the magnitude of changes were much less than during room temperature storage.

Effects of Cigarette Smoke Condensate on the Activities of Xenobiotic Metabolizing Enzymes in Primary Cultured Rat Hepatocytes

  • Park, Mi-Jung;Song, Yeon-Jung;Seo, Kyung-Won
    • Biomolecules & Therapeutics
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    • 제12권3호
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    • pp.185-188
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    • 2004
  • The purpose of this study is to evaluate the effect of cigarette smoke condensate (CSC) on toxification/detoxification metabolic pathway in primary cultured rat hepatocytes. We measured the activities of cytochrome P450 monooxygenases (CYP450s) and UDP-glucuronyltransferase, sulfotransferase and glutathione-S-transferase in CSC-treated rat hepatocytes. CSC significantly increased the activities of hepatic CYP4501A1 and CYP4501A2 to 7.5 fold and 1.6 fold respectively, compared with control level. However, CSC did not affect the activities of conjugation enzymes. We a1so examined if treatment of CSC could change thc cytotoxicity of acetaminophen (AA) through modulation of metabolizing enzymes. In rat hepatocytes, pretreatment with CSC potentiated the cytotoxicity of AA. This result indicates that potentiation of AA toxicity by CSC pretreatment may be related to induction of CYP4501A1 and CYP4501A2.

Glutathione Reductase and Thioredoxin Reductase: Novel Antioxidant Enzymes from Plasmodium berghei

  • Kapoor, Gaurav;Banyal, Harjeet Singh
    • Parasites, Hosts and Diseases
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    • 제47권4호
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    • pp.421-424
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    • 2009
  • Malaria parasites adapt to the oxidative stress during their erythrocytic stages with the help of vital thioredoxin redox system and glutathione redox system. Glutathione reductase and thioredoxin reductase are important enzymes of these redox systems that help parasites to maintain an adequate intracellular redox environment. In the present study, activities of glutathione reductase and thioredoxin reductase were investigated in normal and Plasmodium berghei-infected mice red blood cells and their fractions. Activities of glutathione reductase and thioredoxin reductase in P. berghei-infected host erythrocytes were found to be higher than those in normal host cells. These enzymes were mainly confined to the cytosolic part of cell-free P. berghei. Full characterization and understanding of these enzymes may promise advances in chemotherapy of malaria.

Deinking of ONP with Cellulolytic Enzymes and Synthetic Collecter in Alkaline pH

  • Yoon, Kyong-Dong;Eom, Tae-Jin
    • 한국펄프종이공학회:학술대회논문집
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    • 한국펄프종이공학회 2006년도 PAN PACIFIC CONFERENCE vol.2
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    • pp.451-454
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    • 2006
  • This paper presents an overview of ONP deinking efficiency with cellulolytic enzymes and synthetic collector in alkaline pH. Deinking is a series of unit operations designed to detach ink from cellulose fibers and separate the dispersed ink from the pulp slurry. Deinking chemicals are process aids that enable expensive mill equipment used in these unit operations to operate more efficiently - often much more efficiently. We propose the blended deinking agent with cellulolutic enzymes and synthetic collector in deinking pulp of conventional alkaline method. The deinking efficiency of old news print in alkaline pH was enhanced with enzyme treatments. The brightness of deinked pulp was increased with less residual ink particles and yield of enzymatic deinked pulp was improved compared to the deinked pulp of conventional alkaline method.

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Bioconversion of Lignocellulose Materials

  • Pothiraj, C.;Kanmani, P.;Balaji, P.
    • Mycobiology
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    • 제34권4호
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    • pp.159-165
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    • 2006
  • One of the most economically viable processes for the bioconversion of many lignocellulosic waste is represented by white rot fungi. Phanerochaete chrysosporium is one of the important commercially cultivated fungi which exhibit varying abilities to utilize different lignocellulosic as growth substrate. Examination of the lignocellulolytic enzyme profiles of the two organisms Phanerochaete chrysosporium and Rhizopus stolonifer show this diversity to be reflected in qualitative variation in the major enzymatic determinants (ie cellulase, xylanase, ligninase and etc) required for substrate bioconversion. For example P. chrysosporium which is cultivated on highly lignified substrates such as wood (or) sawdust, produces two extracellular enzymes which have associated with lignin deploymerization. (Mn peroxidase and lignin peroxidase). Conversely Rhizopus stolonifer which prefers high cellulose and low lignin containg substrates produce a family of cellulolytic enzymes including at least cellobiohydrolases and ${\beta}-glucosidases$, but very low level of recognized lignin degrading enzymes.

Rhizobia에서 Malonyl-CoA synthetase와 Malonamidase의 확인 (Identification of Malonate-specific Enzymes, Malonyl-CoA Synthetase and Malonamidase, in Rhizobia)

  • 김유삼;채호준;이은;김용성
    • 미생물학회지
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    • 제29권1호
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    • pp.40-48
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    • 1991
  • Two malonate-specific enzymes, malonyl-CoA synthetase and malonamidase, were found in free-living cultures of Rhizobium japonicum, Rhizobium meliloti, and Rhizobium trifolii, that infect plant roots where contain a high concentration of malonate. Malonyl-CoA synthetase catalyzes the formation of malonyl-CoA, AMP, and PPi directly from malonate, coenzyme A, and ATP in the presence of $Mg^{2+}$ Malonamidase is a novel enzyme that catalyzes hydrolysis and malonyl transfer of malonamate, and forms malonohydroxamate from malonate and hydroxylamine. Both enzymes are highly specific for malonate. These results show that Rhizobia have enzymes able to metabolize malonate and suggest that malonate may be used in symbiotic carbon and nitrogen metabolism.

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인삼엽의 Photobleaching과 항산화효소 활성 (Activities of Antioxidative Enzymes in Photobleaching of Leaves from Panax ginseng C. A. Meyer)

  • 양덕조;이성종
    • Journal of Ginseng Research
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    • 제15권2호
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    • pp.139-143
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    • 1991
  • This study investigated the relations between the photosynthetic rate and the activities of antioxidatile enzymes, glutathione reductase, ascorbate free radical reductase, ascorbate peroxidase, glutathione peroxidase, and ascorbate oxidase, in the leaves of Panax ginseng. Under the normal cultivation condition, Panax in showed lower g1utathione reductase and ascorbate free radical reductase activities the Glycine max. But P ginseng showed higher 91utathione Peroxidase, ascorbate Peroxidase, and ascorbate oxidase activities than C. Panax. Therefore, P. ginseng showed weak activities of reductases for the reduction of the oxidized antioxidants. Under the light intensity of 25 KLux, the reductases showed a decrease of over 75% after 24 hours. But the peroyoxidases decreased about 40%. These results showed that the decrease of reductases acitivities was consistent with the decrease of photosynthetic rate. Therefore, we consider that the regulation of antioxidative enzymes or the application of exogenous antioxidants will be effective means for the protection of photodamage in p. ginseng.

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6-Exomethylenepenam유도체의 베타락타마제 효소억제력과 베타락탐항생제 병용시 활성비교 ($\beta$-Lactamase Inhibitory Activity and Comparative Activity of 6-Exomethylenepenam Derivatives Combined with $\beta$-Lactam Antibiotics)

  • 임채욱;박희석;정미량;강주성;임철부
    • 약학회지
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    • 제47권6호
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    • pp.456-460
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    • 2003
  • In vitro $\beta$-lactamase inhibitory activity of 6-exomethylenepenam compounds ( 1, 2, 3, 4 and 5) was compared with clavulanic acid, sulbactam and tazobactam. The inhibitory activity of compound 3 was stronger than those of sulbactam and clavulanic acid against Type I and II enzymes and stronger than tazobactam against Type III, IV, TEM enzymes. The inhibitory activity of 5 was stronger than sulbactam and clavulanic acid against Type I and II enzymes and stronger than tazobactam against Type III, and IV enzymes. The in vitro antimicrobial activity of 3, 4 and 5 combined with ampicillin and cefoperazone was compared with the sulbactam against $\beta$-lactamase producing 27 strains. But, synergistic activity of 3 and 5 was inferior to tazobactam.

여러 가지 형태에 따른 Alcohol-Oxidase의 특성 비교 (Comparison of the Characteristics of Alcohol-Oxidase by the Various Forms)

  • 이명숙
    • 한국식품영양과학회지
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    • 제22권6호
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    • pp.797-802
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    • 1993
  • The properties of the alcohol-oxidase from yeasts assimilating of methanol(Hansenula polymorpha CBS 4732, Pichia pastoris CBS 2612 and Candida boidinii CBS 8106) as free(cellules, purified enzymes) and immobilized forms(immobilized cellules, immobilized enzymes) were investigated. Immobilization enhanced the activity and stability of alcohol-oxidase to a certain degree. The optimum temperature of the immobilized alcohol-oxidase was lower than those of the free forms. The pH / activi쇼 profiles of alcohol-oxidase did not change by immobilization, but changed by the microorganisms. When the immobilized cellules were stocked at 4$^{\circ}C$ in 10mM potassium phosphate buffer(pH 7.5 or 8.0), alcohol-oxidase was more stable than those were stocked in potassium phosphate buffer containing 0.65M sucrose. The immobilization modifies the conditions of oxidation on the various substrates. alcohol-oxidase in immobilized forms showed some with higher Km value for methanol than that in free ones.

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세포벽 분해효소의 처리에 따른 감과실의 세포벽 성분의 변화 (Changes in the Components of Cell Wall of Persimmon Fruit by Treatments of Cell Wall-Degrading Enzymes)

  • 김광수;신승렬;송준희;김주남
    • 한국식품영양과학회지
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    • 제24권2호
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    • pp.242-246
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    • 1995
  • This paper was carried out to investigate changes in cell wall, cell wall polysaccharides, pectic substances extracted from cell wall of persimmon fruits treated with polygalacturonase and $\beta$-galactosidase in vitro. Degrading degree of cell wall treated with cell wall-degrading enzymes were higher in order polygalacturonase, polygalacturonase+$\beta$-galactosidase and $\beta$-galactosidase. Contents of soluble pectic substances in cell wall treated with cell wall-degrading enzymes showed as the same order as degrading degree of cell wall, while contents of insoluble pectin lower. Contents of versene-soluble pectin and total pectic substance were not affected by cell wall-degrading enzymes. Contents of uronic acid and hexose in soluble material isolated from cell wall treated with polygalacturonase and mixed enzyme were higher than those of untreatment and $\beta$-galactosidase treatment.

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