• Title/Summary/Keyword: enzymes

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Purple Rice Bran Extract Attenuates the Aflatoxin B1-Induced Initiation Stage of Hepatocarcinogenesis by Alteration of Xenobiotic Metabolizing Enzymes

  • Suwannakul, Nattawan;Punvittayagul, Charatda;Jarukamjorn, Kanokwan;Wongpoomchai, Rawiwan
    • Asian Pacific Journal of Cancer Prevention
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    • v.16 no.8
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    • pp.3371-3376
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    • 2015
  • Pigmented rice bran has been suggested to be a valuable source of beneficial phytochemicals. We investigated genotoxic and anti-genotoxic effects of purple rice bran extract (PRBE) in rats using a liver micronucleus assay. Purple rice bran was extracted with methanol, obtaining large amounts of phenolic compounds, including anthocyanins and small amounts of gamma-oryzanol. The experimental protocols were divided into two sets. Male rats were divided into three groups. Group 1 was a negative control, while Groups 2 and 3 were fed with 100 and 500 mg/kg bw of PRBE, respectively, for 28 days. PRBE had no effect on micronucleus formation or xenobiotic metabolizing enzymes in rat liver. Experiments concerning the effect of PRBE on $AFB_1$ showed that PRBE significantly lessened the amount of micronucleated hepatocytes in $AFB_1$ treated rats. Furthermore, it modulated metabolic activation of $AFB_1$ metabolism in the liver by suppressing activity and protein expression of CYP1A2, CYP3A and CYP 450 reductase, and enhancing phase II enzymes including GST and UGT. Overall, purple rice bran extract was not genotoxic in rats. It exhibited anti-genotoxicity by modulation some xenobiotic enzymes active in $AFB_1$ metabolism.

The properties of Proteolytic Enzymes from the Fruit of Broussonetia Kazinoki Siebold (닥나무 열매(楮實子)에서 추출한 단백질 분해효소의 특성에 관한 연구)

  • 윤숙자;오평수;장명숙
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.22 no.6
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    • pp.803-806
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    • 1993
  • The properties of proteolytic enzymes from the fruit of Broussonetia Kazinoki Siebold were investigated. The protease activity of the enzymes from the fruit of Broussonetia Kazinoki Siebold was 1.6 unit. The optimum temperature and pH of the enzymes were $60^{\circ}C$ and 7.0, respectively. The enzymes were stable at pH values from 6 to 8 for 1 hr. at $37^{\circ}C$ of incubation and also retained all activity after incubation for 1 hr. at $60^{\circ}C$. The enzyme preparations showed strong activities toward hemoglobin and collagen.

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Distribution of chitinases and characterization of two chitinolytic enzymes from one-year-old Korean Ginseng (Panax ginseng C.A. Meyer) roots

  • Moon, Jong-Kook;Han, Beom-Ku;Kim, T. Doo-Hun;Jo, Do-Hyun
    • BMB Reports
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    • v.43 no.11
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    • pp.726-731
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    • 2010
  • We report the tissue-specific distribution of chitinolytic activity in Korean ginseng root and characterize two 31-kDa chitinolytic enzymes. These two enzymes (SBF1 and SBF2) were purified 70- and 81-fold with yields of 0.75 and 1.25%, respectively, and exhibited optimal pH and temperature ranges of 5.0-5.5 and 40-$50^{\circ}C$. With [$^3H$]-chitin as a substrate, $K_m$ and $V_{max}$ values of SBF1 were 4.6 mM and 220 mmol/mg-protein/h, respectively, while those of SBF2 were 7.14 mM and 287 mmol/mg-protein/h. The purified enzymes showed markedly less activity with p-nitrophenyl-N-acetylglucosaminide and fluorescent 4-methylumbelliferyl glycosides of D-N-acetylglucosamine oligomers than with [$^3H$]-chitin. End-product inhibition of both enzymes demonstrated that both are endochitinases with different N-acetylglucosaminidase activity. Furthermore, the $NH_2$-terminal sequence of SBF1 showed a high degree of homology with other plant chitinases whereas the $NH_2$-terminal amino acid of SBF2 was blocked.

Partial Characterization of Proteases from Culture Filtrate of Mycobacterium tuberculosis

  • Na, Byoung-Kuk;Song, Chul-Yong;Park, Young-Kill;Bai, Gill-Han;Ki, Sang-Jae
    • Journal of Microbiology
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    • v.34 no.2
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    • pp.198-205
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    • 1996
  • Two proteases were partially characterized from culture filtrate of Mycobacterium, tuberculosis KIT110. Their molecular weights were approximately 200 and 180 kDa, respectively and they exhibited similar enzymatic characteristics. These enzymes were inhibited significantly by EDTA and to some extent by EGTA. Their activity was enhanced by $Ca^{2+}$ and $Mg^{2+}$ to some degree. However, $Cu^{2+}$ and $Ag^{2+}$ completely inhibited the enzyme activity at the concentration of 2.5 and 5 mM, respectively. The optimal pH was 7.0 and optimal temperature was around $40^{\circ}C$. These enzymes were rapidly inactivated at $80^{\circ}C$. Therefore, they were heat-labile, neutral metalloproteases. These enzymes exhibited antigenicity shown by their reacting with sera from the partients with pulmonary tuberculosis. These enzymes were able to degrade serum proteins including hemoglobin, bovine serum albumin, lysozyme and immunoglobulin G and structural matrix protein such as type I collagen. Therefore, these enzymes may be thought to contribute to tissue necrosis and pathogenesis during infection.

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Purification and Characterization of Soymilk-clotting Enzyme Produced by Penicillium sp.

  • Koo, Sung-Keun;Lee, Sang-Ok;Lee, Tae-Ho
    • Journal of Microbiology and Biotechnology
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    • v.2 no.1
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    • pp.14-20
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    • 1992
  • Some microorganisms isolated from soil, including some bacteria and fungi, were found to secrete an extracellular soymilk-clotting enzyme. Among them, an isolated fungus showed the highest soymilk-clotting activity and the strain was assigned to genus Penicillium based on its cultural and morphological characteristics, and designated as Penicillium sp. L-151K. Soymilk-clotting enzymes A and B produced by Penicillium sp. L-151K were purified by ammonium sulfate precipitation and chromatographies on Sephadex G-25, CM-Sephadex, Sephadex G-100 and phenyl-Toyopearl gel. The two purified enzymes A and B were found to be homogeneous by polyacrylamide gel electrophoresis at pH 9.5. The molecular weights of enzyme A and B were 24, 000 and 40, 000, respectively, by gel filtration on Sephadex G-100. Enzymes A and B coagulated soymilk optimally at $60^\circ{C}$ and were stable up to $50^\circ{C}$. Both enzymes were most active at pH 5.8 for soymilk coagulation, and were stable with approximately 80% of original activity from pH 3.0 to 5.0. Each enzyme was an acidic protease with an optimum pH of 3.0 for casein digestion. The soymilk-clotting efficiency of these enzymes was improved with $CaCl_2\;or\;MgCl_2$ when making soymilk-curd.

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Effects of Artemisia iwayomogi Extracts on Antioxidant Enzymes in Rats Administered Benzo($\alpha$) pyrene (쑥 추출물이 Benzo($\alpha$)pyrene을 투여한 흰쥐의 항산화계 효소에 미치는 영향)

  • 정차권;남상명;김종군;함승시;김수진;정명은
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.28 no.1
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    • pp.199-204
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    • 1999
  • This study has attempted to examine the effect of Artemisia iwayomogi extract on antioxidant and liver function related enzymes in rats fed high fat diet along with B( )P administration. The activities of the serum glutamic oxaloacetic transaminase, glutamic pyruvate transaminase and alkaline phosphatase of the rats fed Artemisia iwayomogi ethanol extract were decreased compared to the control. Similarily, the activities of the enzymes were also decreased when the combination of B( )P and ethanol extracts were administered compared to the group adminstered only B( )P. On the other hand, high fat diet increased the above liver function related enzymes. The activities of antioxidant enzymes including GST, catalase and Cu,Zn SOD were significantly increased by feeding the extracts (p<0.01) in addition to the increase of tocopherol contents in the serum. These results suggest that Artemisia iwayomogi extracts can protect cell membranes from the damages by free radicals or hydroperoxides and further may lead to the protection from cancer risks.

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Enzymatic Activity and Distribution of Marker Enzymes between Human Milk and Bovine Milk with Their Separated Milk Fractions (인유 및 우유의 획분에 존재하는 표지효소들의 효소활성과 분포)

  • 조진국;무전안홍;김천제;김창한
    • Food Science of Animal Resources
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    • v.18 no.2
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    • pp.185-191
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    • 1998
  • Human milk and bovine milk in normal stage were fractionated four parts : whey, skimmilk membrane, and casein pellet. The specific activity (nmole / mim / mg protein) and distribution ratio(%) of suborganella marker enzymes in each separated milk fraction were determined. Especially, neutral $Ca^{2+}$-ATPase, acid $Ca^{2+}$-ATPase, NADH-cytochrome C reductase, and acid phosphatase were higher in human milk. However, both $Ca^{2+}$-ATPases were not detected in all fractions of bovine milk. On the other hand, 5'-nucleotidase, phosphodiesterase I, alkaline phosphatase, and $\gamma$-glutamyl transpeptidase activities in bovine milk were higher than in human milk. Most of the marker enzymes were highly distributed in cream fraction of either human milk or bovine milk, and their specific activities were high to 24 fold from 3 fold when compared with that of whole milk. These results suggest that marker enzymes in mammary epitherial cell are transfered into cream fraction by the membrane rearrangement, and different biochemical reaction between human and bovine exists for milk secretion in mammary gland.

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Efficacy Test of Commercial Digestives Containing Antacids, Digestive Enzymes and Herbal Drugs (II)-Digestive Activity Test- (제산제, 소화효소제 및 생약제를 함유한 시판 복합 소화효소제의 효력시험(II)-소화력시험-)

  • Kim, Chong-Koo;Jang, Jung-Yun;Lah, Woon-Young
    • Journal of Pharmaceutical Investigation
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    • v.20 no.4
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    • pp.209-215
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    • 1990
  • The activities of s-amylase, ${\alpha}-amylase$ and protease of three combination products containing digestive enzymes, antacids and herbal drugs on the Korean market were estimated. The effects of antacids and herbal drugs on the activities of digestive enzymes were investigated. Starch-saccarifying activity of s-amylase, starch-dextrinizing activity of ${\alpha}-amylase$ and protein-peptic activity of protease were estimated by Somogy, Mc'Credy, and Casein-Folin method, respectivley. The optimal pH of s-amylase, ${\alpha}-amylase$ and protease were pH 5.0, 4.8 and 7.0, rcspectively. The digestive activities at optimal pH continued about eight hours. The digestive activities of individual enzymes were reduced to 40-90% by antacids and were affected somewhat positively or negatively by herbal drugs. Enzyme activities of the combination products were also affected by pH and reaction time.

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Development of Environmental Stress-Tolerant Plants by Gene Manipulation of Antioxidant Enzymes

  • Kwon, Suk-Yoon;Lee, Haeng-Soon;Kwak, Sang-Soo
    • The Plant Pathology Journal
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    • v.17 no.2
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    • pp.88-93
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    • 2001
  • Oxidative stress is one of the major limiting factor in plant productivity. Reactive oxygens species (ROS) generated during metabolic processes damage cellular functions and consequently lead to disease, senescence and cell death. Plants have evolved an efficient defense system by which the ROS is scavenged by antioxidant enzymes such as superoxide dismutase (SOD) and ascorbate peroxidase (APX). Attempts to reduce oxidative damages under the stress conditions have included the manipulation of 갠 scavenging enzymes by gene transfer technology. Increased SOD activities of transgenic plants lead to increased resistance against oxidative stresses derived from methyl viologen (MV), and from photooxidative damage caused by high light and low temperature. Transgenic tobacco plants overexpressing APX showed reduced damage following either MV treatment of photooxidative treatment. Overexpression of glutathion reductase (GR) leads to increase in pool of ascorbate and GSH, known as small antioxidant molecules. These results indicate through overexpression of enzymes involved in ROS-scavenging could maintain or improve the plant productivities under environment stress condition. In this study, the rational approaches to develop stress-tolerant plants by gene manipulation of antioxidant enzymes will be introduced to provide solutions for the global food and environmental problems in the $21^\textrm{st}$ century.

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Metagenomic Analysis of the Fecal Microbiomes of Wild Asian Elephants Reveals Microflora and Enzymes that Mainly Digest Hemicellulose

  • Zhang, Chengbo;Xu, Bo;Lu, Tao;Huang, Zunxi
    • Journal of Microbiology and Biotechnology
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    • v.29 no.8
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    • pp.1255-1265
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    • 2019
  • To investigate the diversity of gastrointestinal microflora and lignocellulose-degrading enzymes in wild Asian elephants, three of these animals living in the same group were selected for study from the Wild Elephant Valley in the Xishuangbanna Nature Reserve of Yunnan Province, China. Fresh fecal samples from the three wild Asian elephants were analyzed by metagenomic sequencing to study the diversity of their gastrointestinal microbes and cellulolytic enzymes. There were a high abundance of Firmicutes and a higher abundance of hemicellulose-degrading hydrolases than cellulose-degrading hydrolases in the wild Asian elephants. Furthermore, there were a high abundance and a rich diversity of carbohydrate active enzymes (CAZymes) obtained from the gene set annotation of the three samples, with the majority of them showing low identity with the CAZy database entry. About half of the CAZymes had no species source at the phylum or genus level. These indicated that the wild Asian elephants might possess greater ability to digest hemicellulose than cellulose to provide energy, and moreover, the gastrointestinal tracts of these pachyderms might be a potential source of novel efficient lignocellulose-degrading enzymes. Therefore, the exploitation and utilization of these enzyme resources could help us to alleviate the current energy crisis and ensure food security.