• Title/Summary/Keyword: enzyme containing detergent

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Evaluating Bleaching Effects of a Sodium Percarbonate in the Washing Process with Enzyme Containing Detergents (효소세제에 첨가한 과탄산나트륨이 세척효과에 미치는 영향)

  • 정혜원;유지혜;방종호
    • Journal of the Korean Society of Clothing and Textiles
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    • v.26 no.7
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    • pp.1085-1092
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    • 2002
  • Changes in laundering habits and the efficacy claims made for oxygen bleach added to detergents necessitate a deeper investigation into the testing of the washing efficacy of detergents and washing process. The effect of the addition of a sodium percarbonate and bleach activator TAED to an enzyme containing detergent on the soil removal and antimicrobial properties were investigated with the measuring of residual H$_2$O$_2$. The addition of sodium percarbonates to enzyme containing detergent lowered the soil removal of EMPA 116 cloth. But sodium percarbonates had greater effects on that of colored stained cloths such as EMPA 115 and artificially soiled with wine and red pepper while they were presoaked at 20$^{\circ}C$ or higher for So minutes or longer. Most of hydrogen peroxide was remained after washing. Over 99.9% of Staphylococcus aureus on the cotton cloth was removed in every washing solutions, but the cloth washed with enzyme containing detergent or detergent with oxygen bleach didn't show the antimicrobial property.

Molecular Cloning, Characterization, and Application of Organic Solvent-Stable and Detergent-Compatible Thermostable Alkaline Protease from Geobacillus thermoglucosidasius SKF4

  • Suleiman D Allison;Nur AdeelaYasid;Fairolniza Mohd Shariff; Nor'Aini Abdul Rahman
    • Journal of Microbiology and Biotechnology
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    • v.34 no.2
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    • pp.436-456
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    • 2024
  • Several thermostable proteases have been identified, yet only a handful have undergone the processes of cloning, comprehensive characterization, and full exploitation in various industrial applications. Our primary aim in this study was to clone a thermostable alkaline protease from a thermophilic bacterium and assess its potential for use in various industries. The research involved the amplification of the SpSKF4 protease gene, a thermostable alkaline serine protease obtained from the Geobacillus thermoglucosidasius SKF4 bacterium through polymerase chain reaction (PCR). The purified recombinant SpSKF4 protease was characterized, followed by evaluation of its possible industrial applications. The analysis of the gene sequence revealed an open reading frame (ORF) consisting of 1,206 bp, coding for a protein containing 401 amino acids. The cloned gene was expressed in Escherichia coli. The molecular weight of the enzyme was measured at 28 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The partially purified enzyme has its highest activity at a pH of 10 and a temperature of 80℃. In addition, the enzyme showed a half-life of 15 h at 80℃, and there was a 60% increase in its activity at 10 mM Ca2+ concentration. The activity of the protease was completely inhibited (100%) by phenylmethylsulfonyl fluoride (PMSF); however, the addition of sodium dodecyl sulfate (SDS) resulted in a 20% increase in activity. The enzyme was also stable in various organic solvents and in certain commercial detergents. Furthermore, the enzyme exhibited strong potential for industrial use, particularly as a detergent additive and for facilitating the recovery of silver from X-ray film.

Purification and Characterization of Cold Active Lipase from Psychrotrophic Aeromonas sp. LPB 4

  • Lee, Han-Ki;Ahn, Min-Jung;Kwak, Sung-Ho;Song, Won-Ho;Jeong, Byeong-Chul
    • Journal of Microbiology
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    • v.41 no.1
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    • pp.22-27
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    • 2003
  • A lipase from Aeromonas sp. LPB 4, a psychrotophile isolated from a sea sediment was purified and characterized. The lipase was purified 53.5 fold to a homogeneous state by acetone precipitation and QAE sephadex column chromatography and its molecular weight was determined to be 50 kDa by SDS-PAGE. The enzyme exhibited maximum activity at 10$^{\circ}C$ and was stable at temperatures lower than 50$^{\circ}C$. This lipase favored substrates containing medium carbon chain of acyl group, while too low and high carbon chain decreased its activity. The lipolytic activity of purified lipase was slightly increased by the addition of 0.1% detergent, but decreased by 1% of detergent. Butanol severely decreased the lipase activity while methanol increased the activity about 15%.

The Laundry Habits and the Residual Soils of White Cotton Undershirts in Repeating Home Laundry (일반 가정의 세탁 습관 및 반복 세탁에 의한 백색 면 내의의 잔류 오염)

  • 치옥선;이일심
    • Journal of the Korean Society of Clothing and Textiles
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    • v.18 no.4
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    • pp.549-559
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    • 1994
  • The purpose of this study was to study accumlated residual soils which may be one of the causes for yellowing of worn cloths. Wear and wash tests of white cotton undershirts were repeated at 30 households sellected at random over a period of 60 days. Laundry conditions were similar to home laundry habits in a fact-finding survey, using a powdery heavy duty detergent containing no enzymes or enzymes. The subjects in this study were survey of laundry actual condition, the undershirts from prior to and after the final washing was measured residual soils, $L^*a^*b^*$ value and mellowness index of CIE system. D3ta were analysed by simple correlation analysis of wear and wash cycle, residual soils, whiteness The results obtained were summarized as follows: 1. Using pattern of washing machine, Presoaking was no singinificant differnece in general characteristics of survey respondent. Laundry frequency was significant difference in income level, occupation of housewives whether or not. Use of cold and hot water was significant difference in residence shape. 2. The analyzed consequences of recognition and actual behavior in connection with laundry were found variables each other to have independence or not. 3. Amount of residual sebum soils is using non-enzyme detergent were much more than in using enzyme detergent, increased linearly with increase of the number of wear and wash cycles. 4. Residual protein soils with increase of the number wear and wash cycles less than in laundering more easy than sebum soils. Since accumulated residual sebum soils were much more than residual protein soils. 5. Increase of residual soils was raised mellowness index and diminshed whiteness. yellowness index of residual sebum soils was higher than protein soils. If increase of whiteness will be incresed, amount of residual sebum soils will be decreased sebum soils. Because amount of residual sebum soils much more than protein soils, yellowness index of residual sebum soils was more higher than that of protein soils.

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Interaction of Stomatin with Hepatitis C Virus RNA Polymerase Stabilizes the Viral RNA Replicase Complexes on Detergent-Resistant Membranes

  • Kim, Jung-Hee;Rhee, Jin-Kyu;Ahn, Dae-Gyun;Kim, Kwang Pyo;Oh, Jong-Won
    • Journal of Microbiology and Biotechnology
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    • v.24 no.12
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    • pp.1744-1754
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    • 2014
  • The hepatitis C virus (HCV) RNA genome is replicated by an RNA replicase complex (RC) consisting of cellular proteins and viral nonstructural (NS) proteins, including NS5B, an RNA-dependent RNA polymerase (RdRp) and key enzyme for viral RNA genome replication. The HCV RC is known to be associated with an intracellular membrane structure, but the cellular components of the RC and their roles in the formation of the HCV RC have not been well characterized. In this study, we took a proteomic approach to identify stomatin, a member of the integral proteins of lipid rafts, as a cellular protein interacting with HCV NS5B. Co-immunoprecipitation and co-localization studies confirmed the interaction between stomatin and NS5B. We demonstrated that the subcellular fraction containing viral NS proteins and stomatin displays RdRp activity. Membrane flotation assays with the HCV genome replication-competent subcellular fraction revealed that the HCV RdRp and stomatin are associated with the lipid raft-like domain of membranous structures. Stomatin silencing by RNA interference led to the release of NS5B from the detergent-resistant membrane, thereby inhibiting HCV replication in both HCV subgenomic replicon-harboring cells and HCV-infected cells. Our results identify stomatin as a cellular protein that plays a role in the formation of an enzymatically active HCV RC on a detergent-resistant membrane structure.

Expression and Biochemical Characteristics of a Phospholipase D from Bacillus licheniformis (Bacillus licheniformis로부터 분리된 phospholipase D 유전자의 발현 및 생화학 특성)

  • Kang, Han-Chul;Yoon, Sang-Hong;Lee, Chang-Muk;Koo, Bon-Sung
    • Journal of Applied Biological Chemistry
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    • v.54 no.2
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    • pp.94-100
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    • 2011
  • A gene encoding a putative phospholipase D was isolated from Bacillus licheniformis and cloned into pGEM-T easy vector. The gene was expressed in E. coli BL21 (DE3) using a pET-21(a) vector containing His6 tag. Affinity purification of the recombinant phospholipase D with nickel-nitrilotriacetic acid (Ni-NTA) resin resulted major one-band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The purified enzyme showed a molecular weight of 44 kDa. The optimum activity of enzyme was around pH 7.0 and the enzyme was also the most stable around this condition. The optimum temperature was about $40-45^{\circ}C$ and the enzyme still showed considerable activities at wide range of temperature. Among various detergents, Triton X-100 significantly increased the enzyme activity, resulting in 181% activity of control at 0.6 mM of the detergent. Calcium ion did not significantly affect the enzyme activity, suggesting that the enzyme might be classified into $Ca^{2+}$-independent PLD.

Development of Membrane Strip Assay System for Lipoprotein Cholesterol Based on Liquid-Phase Enzyme Reactions (액상 효소반응을 이용한 Membrane Strip 형 Cholesterol 측정시스템의 개발)

  • 신인수;목락선;장미라;백세환
    • KSBB Journal
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    • v.13 no.5
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    • pp.577-584
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    • 1998
  • A sensitive membrane strip assay for plasma lipoprotein cholesterol that can be performed without handling reagents has been investigated. We previously developed an assay system with immobilized enzymes (cholesterol esterase and cholesterol oxidase) on the surfaces of nitrocellulose membrane(1). In such a case, the amount of enzymes present on the membrane was limited by its surface area and, thus, the detection capability was relatively poor (> 50 mg/dL cholesterol). To overcome this problem, we devised a new system with non-immobilized enzymes by placing them within interstitial spaces of a celullose membrane pad in a dry state. Upon contact with sample medium, the enzymes were immediately dissolved and participated in the reactions with cholesterol in a liquid phase. We constructed a user-friendly system consisting of four membrane pads fro sample application, cholesterol decomposition, color development as signal, and medium absorption to invoke a continuous flow (sequential location from the bottom). A sample containing lipoproteins was added into the application pad by capillary action and transferred to the next pad for decomposition. The decomposition pad (namely, enzyme pad) contained a detergent (sodium cholate) for the destruction of lipoprotein particles, the two enzymes for cholesterol decomposition, and a chromogen (3,3'-diaminobenzidine). As a consequence of the enzyme reactions, hydrogen peroxide was produced, and then reacted in the presence of the chromogen with horseradish peroxidase immobilized on the signal generation pad. Finally, a colorimetric signal directly proportional to the cholesterol concentration was produced. The detection limit determined from this system under optimal conditions was at least 2 times lower than of the enzyme-immobilized system.

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Cloning of a Alkaline Protease Gene from Xanthomonas sp. YL-37 (Xanthomonas sp. YL-37의 Alkaline Protease 유전자의 클로닝)

  • 이대희;김수경;이승철;윤병대;황용일
    • Microbiology and Biotechnology Letters
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    • v.23 no.2
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    • pp.145-149
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    • 1995
  • For the purpose of developing a new biodegradable detergent, we have isolated a gene encoding wide-range temperature applicable alkaline protease from Xanthomonas sp. YL-37 (Lee et al., 1994, Kor. J. Appl. Microbiol. Biotechnol.). An alkaline protease gene was isolated from the gene bank that was prepared from the chromosomal DNA of Xanthomonas sp. YL-37. From the results of agarose gel electrophoresis and a restriction enzyme mapping, a 2.7 kb DNA fragment containing the alkaline protease gene was inserted in the plasmid pUC9. Extracellular activity of a clone having alkaline protease gene was detected on SDS-polyacrylamide gel with activity staining assay. The molecular weight of alkaline protease was determined to be about 64 kDa from 11% SDS-PAGE analysis. Alkaline protease activity, produced from E. coli which harboring the plasmid, showed no difference at reaction temperature 20, 30 and 40$\circ$C, respectively. This result showed that alkaline protease produced from E. coli harboring the plasmid was apparently the same as that of Xanthomonas sp. YL-37.

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Substitution of Wheat for Corn in Beef Cattle Diets: Digestibility, Digestive Enzyme Activities, Serum Metabolite Contents and Ruminal Fermentation

  • Liu, Y.F.;Zhao, H.B.;Liu, X.M.;You, W.;Cheng, H.J.;Wan, F.C.;Liu, G.F.;Tan, X.W.;Song, E.L.;Zhang, X.L.
    • Asian-Australasian Journal of Animal Sciences
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    • v.29 no.10
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    • pp.1424-1431
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    • 2016
  • The objective of this study was to evaluate the effect of diets containing different amounts of wheat, as a partial or whole substitute for corn, on digestibility, digestive enzyme activities, serum metabolite contents and ruminal fermentation in beef cattle. Four Limousin${\times}$LuXi crossbred cattle with a body weight ($400{\pm}10kg$), fitted with permanent ruminal, proximal duodenal and terminal ileal cannulas, were used in a $4{\times}4$ Latin square design with four treatments: Control (100% corn), 33% wheat (33% substitution for corn), 67% wheat (67% substitution for corn), and 100% wheat (100% substitution for corn) on a dry matter basis. The results showed that replacing corn with increasing amounts of wheat increased the apparent digestibility values of dry matter, organic matter, and crude protein (p<0.05). While the apparent digestibility of acid detergent fiber and neutral detergent fiber were lower with increasing amounts of wheat. Digestive enzyme activities of lipase, protease and amylase in the duodenum were higher with increasing wheat amounts (p<0.05), and showed similar results to those for the enzymes in the ileum except for amylase. Increased substitution of wheat for corn increased the serum alanine aminotransferase concentration (p<0.05). Ruminal pH was not different between those given only corn and those given 33% wheat. Increasing the substitution of wheat for corn increased the molar proportion of acetate and tended to increase the acetate-to-propionate ratio. Cattle fed 100% wheat tended to have the lowest ruminal $NH_3-N$ concentration compared with control (p<0.05), whereas no differences were observed among the cattle fed 33% and 67% wheat. These findings indicate that wheat can be effectively used to replace corn in moderate amounts to meet the energy and fiber requirements of beef cattle.

Influence of Palm Kernel Meal Inclusion and Exogenous Enzyme Supplementation on Growth Performance, Energy Utilization, and Nutrient Digestibility in Young Broilers

  • Abdollahi, M.R.;Hosking, B.J.;Ning, D.;Ravindran, V.
    • Asian-Australasian Journal of Animal Sciences
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    • v.29 no.4
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    • pp.539-548
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    • 2016
  • The objective of the present study was to investigate the influence of palm kernel meal (PKM) inclusion and exogenous enzyme supplementation on growth performance, nitrogen-corrected apparent metabolizable energy (AMEn), coefficient of apparent ileal digestibility (CAID) and total tract retention of nutrients in young broilers fed corn-based diets. Four inclusion levels of PKM (no PKM [PKM0], 8% [PKM8], 16% [PKM16], and 24% [PKM24]) and two enzyme additions were evaluated in a $4{\times}2$ factorial arrangement of treatments. A total of 384, one-d-old male broilers (Ross 308) were individually weighed and allocated to 48 cages (eight broilers/cage), and cages were randomly assigned to eight dietary treatments. Results indicated that the inclusion of 8% and 16% PKM increased (p<0.05) the weight gain compared to the PKM0 diet. Birds fed the PKM8 diets had the highest (p<0.05) feed intake. Weight gain and feed intake were severely reduced (p<0.05) by feeding the PKM24 diet. Enzyme supplementation increased weight gain (p<0.05), independent of PKM inclusion level. In PKM0 and PKM8 diets, enzyme addition significantly (p<0.05) lowered feed conversion ratio (FCR); whereas enzyme addition had no effect on FCR of birds fed PKM16 and PKM24 diets. In PKM0 and PKM16 diets, enzyme addition significantly (p<0.05) increased CAID of nitrogen and energy but had no effect in the PKM8 and PKM24 diets. Inclusion of PKM into the basal diet, irrespective of inclusion level, enhanced (p<0.05) starch and fat digestibility. Inclusion of PKM at 16% and 24% resulted in similar CAID of neutral detergent fiber (NDF) but higher (p<0.05) than that of the PKM0 and PKM8 diets. Enzyme addition, regardless of the level of PKM inclusion, significantly (p<0.05) increased CAID of NDF. There was a significant (p<0.05) decrease in AMEn with PKM inclusion of 24%. The present data suggest that inclusion of PKM in broiler diets could be optimized if PKM-containing diets are formulated based on digestible amino acid contents and supplemented with exogenous enzymes. If amino acid digestibility and AME of PKM considered in the formulation, it can be included in broiler diets up to 16% with no deleterious effects on growth performance.