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In particular, a number of physicochemical factors important in defining the surface at the molecular level were assessed for their effect on the adhesion of\n            \u003Cjats:italic>Listeria monocytogenes\u003C\u002Fjats:italic>\n            ,\n            \u003Cjats:italic>Salmonella typhimurium\u003C\u002Fjats:italic>\n            ,\n            \u003Cjats:italic>Staphylococcus aureus\u003C\u002Fjats:italic>\n            , and\n            \u003Cjats:italic>Escherichia coli\u003C\u002Fjats:italic>\n            . The primary experiments involved the grafting of groups varying in hydrophilicity, hydrophobicity, chain length, and chemical functionality onto glass substrates such that the surfaces were homogeneous and densely packed with functional groups. All of the surfaces were found to be chemically well defined, and their measured surface energies varied from 15 to 41 mJ · m\n            \u003Cjats:sup>−2\u003C\u002Fjats:sup>\n            . Protein adsorption experiments were performed with\n            \u003Cjats:sup>3\u003C\u002Fjats:sup>\n            H-labelled bovine serum albumin and cytochrome\n            \u003Cjats:italic>c\u003C\u002Fjats:italic>\n            prior to bacterial attachment studies. Hydrophilic uncharged surfaces showed the greatest resistance to protein adsorption; however, our studies also showed that the effectiveness of poly(ethyleneoxide) (PEO) polymers was not simply a result of its hydrophilicity and molecular weight alone. The adsorption of the two proteins approximately correlated with short-term cell adhesion, and bacterial attachment for\n            \u003Cjats:italic>L. monocytogenes\u003C\u002Fjats:italic>\n            and\n            \u003Cjats:italic>E. coli\u003C\u002Fjats:italic>\n            also correlated with the chemistry of the underlying substrate. However, for\n            \u003Cjats:italic>S. aureus\u003C\u002Fjats:italic>\n            and\n            \u003Cjats:italic>S. typhimurium\u003C\u002Fjats:italic>\n            a different pattern of attachment occurred, suggesting a dissimilar mechanism of cell attachment, although high-molecular-weight PEO was still the least-cell-adsorbing surface. The implications of this for in vivo attachment of cells suggest that hydrophilic passivating groups may be the best method for preventing cell adsorption to synthetic substrates provided they can be grafted uniformly and in sufficient density at the surface.\n          \u003C\u002Fjats:p>",{"EN":128},"Bacterial Adhesion at Synthetic Surfaces",{"VOID":130},"10543814",{"VOID":132},"10.1128\u002Faem.65.11.4995-5002.1999","PUBLICATION","VERIFIED","2024-12-10T17:23:10.233+00:00","Auto Verify",[138],"EN","https:\u002F\u002Fjournals.asm.org\u002Fdoi\u002F10.1128\u002FAEM.65.11.4995-5002.1999",[141,158,174,194],{"id":142,"sortIndex":25,"researcher":24,"roles":143,"affiliations":144,"properties":153,"displayName":155,"givenName":24,"familyName":24},"b621752d-d7e2-4c21-86c0-fada9cabbd68",[],[145],{"id":146,"sortIndex":25,"affiliation":147,"properties":24},"dae97509-0418-4b7f-919d-fcd8277c1c5a",{"id":146,"createTime":24,"updateTime":24,"relativeEntities":148,"slug":24,"properties":149,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":152,"statistic":24},[],{"title":150},{"EN":151},"Macromolecular Science Department, Institute of Food Research, Reading Laboratory, Reading RG6 6BZ, United Kingdom",[],{"title":154,"openalex":156},{"EN":155},"David Cunliffe",{"VOID":157},"A5031825062",{"id":159,"sortIndex":160,"researcher":24,"roles":161,"affiliations":162,"properties":169,"displayName":171,"givenName":24,"familyName":24},"f9cbf720-3960-4f89-88dd-c3e03a1ffcec",1,[],[163],{"id":146,"sortIndex":25,"affiliation":164,"properties":24},{"id":146,"createTime":24,"updateTime":24,"relativeEntities":165,"slug":24,"properties":166,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":168,"statistic":24},[],{"title":167},{"EN":151},[],{"title":170,"openalex":172},{"EN":171},"Christopher A. 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C.\nAdsorption of microorganisms to surfaces.\n1980\nJohn Wiley & Sons\nLondon England",{"doi":301},"10.1097\u002F00010694-198011000-00012",{"id":24,"text":303,"url":24,"identifiers":304},"10.1016\u002F0924-2244(96)81255-6",{"doi":303},{"id":24,"text":306,"url":24,"identifiers":307},"Brady R. F. In search of non-stick coatings. Chem. Indust. 6 1997 219 222",{},{"id":24,"text":309,"url":24,"identifiers":310},"10.1016\u002F0964-8305(94)90092-2",{"doi":309},{"id":24,"text":312,"url":24,"identifiers":313},"10.1002\u002Fbit.260230902",{"doi":312},{"id":24,"text":315,"url":24,"identifiers":316},"10.1021\u002Fla00013a022",{"doi":315},{"id":24,"text":318,"url":24,"identifiers":319},"10.1146\u002Fannurev.ms.26.080196.002053",{"doi":318},{"id":24,"text":321,"url":24,"identifiers":322},"10.1042\u002Fbj3250229",{"doi":321},{"id":24,"text":324,"url":24,"identifiers":325},"10.1016\u002F0168-3659(94)90041-8",{"doi":324},{"id":24,"text":327,"url":24,"identifiers":328},"10.1016\u002F0166-6622(86)80088-9",{"doi":327},{"id":24,"text":330,"url":24,"identifiers":331},"10.1002\u002Fjbm.820251211",{"doi":330},{"id":24,"text":333,"url":24,"identifiers":334},"10.1016\u002F0003-2697(89)90426-0",{"doi":333},{"id":24,"text":336,"url":24,"identifiers":337},"Hamilton\nW.\nCharacklis\nW. G.\nRelative activities of cells in suspension and in biofilms\nStructure and function of biofilms.\nCharacklis\nW. G.\nWilderer\nP. A.\n1989\n199\n219\nJohn Wiley\nNew York N.Y",{},{"id":24,"text":339,"url":24,"identifiers":340},"10.1021\u002Fjp972635z",{"doi":339},{"id":24,"text":342,"url":24,"identifiers":343},"10.1016\u002F0956-7135(95)91449-U",{"doi":342},{"id":24,"text":345,"url":24,"identifiers":346},"10.1111\u002Fj.1574-6968.1996.tb08408.x",{"doi":345},{"id":24,"text":348,"url":24,"identifiers":349},"10.1046\u002Fj.1432-1327.1998.2580897.x",{"doi":348},{"id":24,"text":351,"url":24,"identifiers":352},"10.1002\u002Fjbm.820290609",{"doi":351},{"id":24,"text":354,"url":24,"identifiers":355},"10.1021\u002Fla9505879",{"doi":354},{"id":24,"text":357,"url":24,"identifiers":358},"10.1016\u002FS0006-3495(94)80938-5",{"doi":357},{"id":24,"text":360,"url":24,"identifiers":361},"10.1016\u002F0079-6700(95)00011-4",{"doi":360},{"id":24,"text":363,"url":24,"identifiers":364},"10.1099\u002F00221287-68-3-337",{"doi":363},{"id":24,"text":366,"url":24,"identifiers":367},"Melo\nL. F.\nBott\nT. R.\nFletcher\nM.\nCapdeville\nB.\nBiofilms-science and technology.\n1992\nKluwer Academic Press\nDordrecht The Netherlands",{"doi":368},"10.1007\u002F978-94-011-1824-8",{"id":24,"text":370,"url":24,"identifiers":371},"10.3109\u002F10408419609106456",{"doi":370},{"id":24,"text":373,"url":24,"identifiers":374},"10.1163\u002F156856297X00263",{"doi":373},{"id":24,"text":376,"url":24,"identifiers":377},"10.1016\u002F0964-8305(94)90083-3",{"doi":376},{"id":24,"text":379,"url":24,"identifiers":380},"10.1016\u002F0001-8686(86)80012-4",{"doi":379},{"id":24,"text":382,"url":24,"identifiers":383},"Schackenraad J. M. Stokroos I. Bartels H. Busscher H. J. Patency of small calibre, superhydrophobic E-PTFE vascular grafts: a pilot-study in rabbit carotid artery. Cells Mater. 2 1992 193 199",{},{"id":24,"text":385,"url":24,"identifiers":386},"10.1006\u002Fjcis.1996.4748",{"doi":385},{"id":24,"text":388,"url":24,"identifiers":389},"10.1021\u002Fma971016l",{"doi":388},{"id":24,"text":391,"url":24,"identifiers":392},"10.1006\u002Fjcis.1993.1044",{"doi":391},{"id":24,"text":394,"url":24,"identifiers":395},"10.1016\u002F0021-9797(91)90139-Y",{"doi":394},{"id":24,"text":397,"url":24,"identifiers":398},"10.1007\u002FBF00878244",{"doi":397},{"id":24,"text":400,"url":24,"identifiers":401},"10.1021\u002Fcr00088a006",{"doi":400},{"id":24,"text":403,"url":24,"identifiers":404},"10.1021\u002Fbk-1997-0680.ch001",{"doi":403},{"id":24,"text":406,"url":24,"identifiers":407},"10.1016\u002F0168-1605(94)90047-7",{"doi":406},false,{"id":410,"createTime":411,"updateTime":412,"relativeEntities":413,"slug":414,"properties":415,"entityType":133,"verifyStatus":134,"verifyTime":432,"verifyNote":136,"languages":433,"translateLanguages":24,"viewCount":25,"primaryUrl":434,"fullTextUrl":24,"authors":435,"publicationType":210,"publisherRelationship":525,"citationCount":581,"citationInfo":582,"publishDate":585,"publishYear":583,"citationAnalyzeStatus":282,"lastCitationAnalyze":586,"indexDatabases":587,"openAccess":24,"references":588,"isForceReanalyzing":408},"cf651b10-482d-40d6-8113-7ea3c2701879","2024-12-21T22:30:02.892+00:00","2026-07-24T10:21:01.550+00:00",[],"Compartmentalization-of-the-Carbaryl-Degradation-Pathway-Molecular-Characterization-of-Inducible-Periplasmic-Carbaryl-Hydrolase-from-Pseudomonas-spp",{"mag":416,"gsPaper":418,"pmc":420,"openalex":422,"abstract":424,"title":426,"pm":428,"doi":430},{"VOID":417},"2765684095",{"VOID":419},"[\"9445641910564406961\"]",{"VOID":421},"5752863",{"VOID":423},"W2765684095",{"EN":425},"\u003Cjats:title>ABSTRACT\u003C\u002Fjats:title>\n          \u003Cjats:p>\n            \u003Cjats:named-content content-type=\"genus-species\">Pseudomonas\u003C\u002Fjats:named-content>\n            sp. strains C5pp and C7 degrade carbaryl as the sole carbon source. Carbaryl hydrolase (CH) catalyzes the hydrolysis of carbaryl to 1-naphthol and methylamine. Bioinformatic analysis of\n            \u003Cjats:italic>mcbA\u003C\u002Fjats:italic>\n            , encoding CH, in C5pp predicted it to have a transmembrane domain (Tmd) and a signal peptide (Sp). In these isolates, the activity of CH was found to be 4- to 6-fold higher in the periplasm than in the cytoplasm. The recombinant CH (rCH) showed 4-fold-higher activity in the periplasm of\n            \u003Cjats:named-content content-type=\"genus-species\">Escherichia coli\u003C\u002Fjats:named-content>\n            . The deletion of Tmd showed activity in the cytoplasmic fraction, while deletion of both Tmd and Sp (Tmd+Sp) resulted in expression of the inactive protein. Confocal microscopic analysis of\n            \u003Cjats:named-content content-type=\"genus-species\">E. coli\u003C\u002Fjats:named-content>\n            expressing a (Tmd+Sp)-green fluorescent protein (GFP) fusion protein revealed the localization of GFP into the periplasm. Altogether, these results indicate that Tmd probably helps in anchoring of polypeptide to the inner membrane, while Sp assists folding and release of CH in the periplasm. The N-terminal sequence of the mature periplasmic CH confirms the absence of the Tmd+Sp region and confirms the signal peptidase cleavage site as Ala-Leu-Ala. CH purified from strains C5pp, C7, and rCHΔ(Tmd)a were found to be monomeric with molecular mass of ∼68 to 76 kDa and to catalyze hydrolysis of the ester bond with an apparent\n            \u003Cjats:italic>\n              K\n              \u003Cjats:sub>m\u003C\u002Fjats:sub>\n            \u003C\u002Fjats:italic>\n            and\n            \u003Cjats:italic>V\u003C\u002Fjats:italic>\n            \u003Cjats:sub>max\u003C\u002Fjats:sub>\n            in the range of 98 to 111 μM and 69 to 73 μmol · min\n            \u003Cjats:sup>−1\u003C\u002Fjats:sup>\n            · mg\n            \u003Cjats:sup>−1\u003C\u002Fjats:sup>\n            , respectively. The presence of low-affinity CH in the periplasm and 1-naphthol-metabolizing enzymes in the cytoplasm of\n            \u003Cjats:named-content content-type=\"genus-species\">Pseudomonas\u003C\u002Fjats:named-content>\n            spp. suggests the compartmentalization of the metabolic pathway as a strategy for efficient degradation of carbaryl at higher concentrations without cellular toxicity of 1-naphthol.\n          \u003C\u002Fjats:p>\n          \u003Cjats:p>\n            \u003Cjats:bold>IMPORTANCE\u003C\u002Fjats:bold>\n            Proteins in the periplasmic space of bacteria play an important role in various cellular processes, such as solute transport, nutrient binding, antibiotic resistance, substrate hydrolysis, and detoxification of xenobiotics. Carbaryl is one of the most widely used carbamate pesticides. Carbaryl hydrolase (CH), the first enzyme of the degradation pathway which converts carbaryl to 1-naphthol, was found to be localized in the periplasm of\n            \u003Cjats:named-content content-type=\"genus-species\">Pseudomonas\u003C\u002Fjats:named-content>\n            spp. Predicted transmembrane domain and signal peptide sequences of\n            \u003Cjats:named-content content-type=\"genus-species\">Pseudomonas\u003C\u002Fjats:named-content>\n            were found to be functional in\n            \u003Cjats:named-content content-type=\"genus-species\">Escherichia coli\u003C\u002Fjats:named-content>\n            and to translocate CH and GFP into the periplasm. The localization of low-affinity CH into the periplasm indicates controlled formation of toxic and recalcitrant 1-naphthol, thus minimizing its accumulation and interaction with various cellular components and thereby reducing the cellular toxicity. This study highlights the significance of compartmentalization of metabolic pathway enzymes for efficient removal of toxic compounds.\n          \u003C\u002Fjats:p>",{"EN":427},"Compartmentalization of the Carbaryl Degradation Pathway: Molecular Characterization of Inducible Periplasmic Carbaryl Hydrolase from Pseudomonas spp",{"VOID":429},"29079626",{"VOID":431},"10.1128\u002Faem.02115-17","2024-12-21T22:30:02.891+00:00",[138],"https:\u002F\u002Fjournals.asm.org\u002Fdoi\u002F10.1128\u002FAEM.02115-17",[436,453,472,491,508],{"id":437,"sortIndex":25,"researcher":24,"roles":438,"affiliations":439,"properties":448,"displayName":450,"givenName":24,"familyName":24},"f3004fbd-52a4-4b2f-a5ad-5dd9b13fcfdc",[],[440],{"id":441,"sortIndex":25,"affiliation":442,"properties":24},"9611c15d-2e8a-431d-9cbe-5821512a3c5b",{"id":441,"createTime":24,"updateTime":24,"relativeEntities":443,"slug":24,"properties":444,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":447,"statistic":24},[],{"title":445},{"EN":446},"Department of Biosciences and Bioengineering, Indian Institute of Technology-Bombay, Powai, Mumbai, India",[],{"title":449,"openalex":451},{"EN":450},"Kamini",{"VOID":452},"A5021941083",{"id":454,"sortIndex":160,"researcher":24,"roles":455,"affiliations":456,"properties":463,"displayName":467,"givenName":24,"familyName":24},"60af1cc7-a3fe-4019-a751-35d91e0723fd",[],[457],{"id":441,"sortIndex":25,"affiliation":458,"properties":24},{"id":441,"createTime":24,"updateTime":24,"relativeEntities":459,"slug":24,"properties":460,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":462,"statistic":24},[],{"title":461},{"EN":446},[],{"orcid":464,"title":466,"gsAuthor":468,"openalex":470},{"VOID":465},"https:\u002F\u002Forcid.org\u002F0000-0001-8778-3615",{"EN":467},"Dasvit Shetty",{"VOID":469},"[\"S2ZwaRMAAAAJ\"]",{"VOID":471},"A5040943750",{"id":473,"sortIndex":176,"researcher":24,"roles":474,"affiliations":475,"properties":482,"displayName":486,"givenName":24,"familyName":24},"1d6f8525-459b-45b0-98a4-b2025eb5c55d",[],[476],{"id":441,"sortIndex":25,"affiliation":477,"properties":24},{"id":441,"createTime":24,"updateTime":24,"relativeEntities":478,"slug":24,"properties":479,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":481,"statistic":24},[],{"title":480},{"EN":446},[],{"orcid":483,"title":485,"gsAuthor":487,"openalex":489},{"VOID":484},"https:\u002F\u002Forcid.org\u002F0000-0002-2703-8311",{"EN":486},"Vikas D. 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Toxicology of organophosphate and carbamate compounds. Academic Press Inc., New York, NY.",{},{"id":24,"text":683,"url":24,"identifiers":684},"Oliver DB. 1996. Periplasm, p 88–103. In Neidhardt FC, Curtiss R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. 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This element encodes site-specific integrase and excisionase enzymes related to those of conjugative transposons Tn\n            \u003Cjats:italic>5276\u003C\u002Fjats:italic>\n            and Tn\n            \u003Cjats:italic>5252\u003C\u002Fjats:italic>\n            . The integrase was found to be involved in a site-specific excision of a circular form. ICE\n            \u003Cjats:italic>St1\u003C\u002Fjats:italic>\n            also encodes putative conjugative transfer proteins related to those of the conjugative transposon Tn\n            \u003Cjats:italic>916\u003C\u002Fjats:italic>\n            . Therefore, ICE\n            \u003Cjats:italic>St1\u003C\u002Fjats:italic>\n            could be or could be derived from an integrative conjugative element.\n          \u003C\u002Fjats:p>",{"EN":745},"Characterization of a Novel Integrative Element, ICE\n            \u003Ci>St1\u003C\u002Fi>\n            , in the Lactic Acid Bacterium\n            \u003Ci>Streptococcus 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Borer P. N. Dengler B. Levin M. D. Uhlenbeck O. C. Crothers D. M. Bralla J. Improved estimation of secondary structure in ribonucleic acids. 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It is applied as a preservative in various food products. The solubility and stability of nisin and nisin mutants have been studied. It is demonstrated that nisin mutants can be produced with improved functional properties. The solubility of nisin A is highest at low pH values and gradually decreases by almost 2 orders of magnitude when the pH of the solution exceeds a value of 7. At low pH, nisin Z exhibits a decreased solubility relative to that of nisin A; at neutral and higher pH values, the solubilities of both variants are comparable. Two mutants of nisin Z, which contain lysyl residues at positions 27 and 31, respectively, instead of Asn-27 and His-31, were produced with the aim of reaching higher solubility at neutral pH. Both mutants were purified to homogeneity, and their structures were confirmed by one- and two-dimensional 1H nuclear magnetic resonance. Their antimicrobial activities were found to be similar to that of nisin Z, whereas their solubilities at pH 7 increased by factors of 4 and 7, respectively. The chemical stability of nisin A was studied in the pH range of 2 to 8 and at a 20, 37, and 75 degrees C. Optimal stability was observed at pH 3.0. Nisin Z showed a behavior similar to that of nisin A. A mutant containing dehydrobutyrine at position 5 instead of dehydroalanine had lower activity but was significantly more resistant to acid-catalyzed chemical degradation than wild-type nisin Z.\u003C\u002Fjats:p>",{"EN":1012},"Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering",{"VOID":1014},"7487019",{"VOID":1016},"10.1128\u002Faem.61.8.2873-2878.1995",[138],"https:\u002F\u002Fjournals.asm.org\u002Fdoi\u002F10.1128\u002Faem.61.8.2873-2878.1995",[1020,1037,1056,1071,1088],{"id":1021,"sortIndex":25,"researcher":24,"roles":1022,"affiliations":1023,"properties":1032,"displayName":1034,"givenName":24,"familyName":24},"92983958-519a-479d-b1c2-e45995357c5c",[],[1024],{"id":1025,"sortIndex":25,"affiliation":1026,"properties":24},"efe49c93-841e-4382-8996-d342910c7178",{"id":1025,"createTime":24,"updateTime":24,"relativeEntities":1027,"slug":24,"properties":1028,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":1031,"statistic":24},[],{"title":1029},{"VI":1030},"Department of Biophysical Chemistry, Netherlands Institute for Dairy Research (NIZO), Ede.",[],{"title":1033,"openalex":1035},{"EN":1034},"Harry S. 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The pressure resistance of stationary-phase cells was much higher than that of exponential-phase cells, but in both types of cell, aggregation of cytoplasmic proteins and condensation of the nucleoid occurred after treatment at 200 MPa for 8 min. Although gross changes were detected in these cellular structures, they were not related to cell death, at least for stationary-phase cells. In addition to these events, exponential-phase cells showed changes in their cell envelopes that were not seen for stationary-phase cells, namely physical perturbations of the cell envelope structure, a loss of osmotic responsiveness, and a loss of protein and RNA to the extracellular medium. Based on these observations, we propose that exponential-phase cells are inactivated under high pressure by irreversible damage to the cell membrane. In contrast, stationary-phase cells have a cytoplasmic membrane that is robust enough to withstand pressurization up to very intense treatments. The retention of an intact membrane appears to allow the stationary-phase cell to repair gross changes in other cellular structures and to remain viable at pressures that are lethal to exponential-phase cells.\n          \u003C\u002Fjats:p>",{"EN":1187},"Morphological and Physiological Changes Induced by High Hydrostatic Pressure in Exponential- and Stationary-Phase Cells of\n            \u003Ci>Escherichia coli\u003C\u002Fi>\n            : Relationship with Cell Death",{"VOID":1189},"15006777",{"VOID":1191},"10.1128\u002Faem.70.3.1545-1554.2004","2024-09-20T11:07:13.729+00:00",[138],"https:\u002F\u002Fjournals.asm.org\u002Fdoi\u002F10.1128\u002FAEM.70.3.1545-1554.2004",[1196,1215],{"id":1197,"sortIndex":25,"researcher":24,"roles":1198,"affiliations":1199,"properties":1208,"displayName":1212,"givenName":24,"familyName":24},"366f75e9-a39c-40eb-bea5-012dc2515554",[],[1200],{"id":1201,"sortIndex":25,"affiliation":1202,"properties":24},"cd428b47-4d7c-4d66-ba5f-604280b66fd5",{"id":1201,"createTime":24,"updateTime":24,"relativeEntities":1203,"slug":24,"properties":1204,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":1207,"statistic":24},[],{"title":1205},{"EN":1206},"School of Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AP, United Kingdom",[],{"orcid":1209,"title":1211,"openalex":1213},{"VOID":1210},"https:\u002F\u002Forcid.org\u002F0000-0002-7971-4828",{"EN":1212},"P. 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A., and R. J. Stretton. 1981. Effect of growth medium on the lipid composition of log and stationary phase cultures of Salmonella typhimurium.Microbios31:161-170.",{},{"id":24,"text":1326,"url":24,"identifiers":1327},"10.1046\u002Fj.1365-2958.1999.01425.x",{"doi":1326},{"id":24,"text":1329,"url":24,"identifiers":1330},"10.4315\u002F0362-028X-62.11.1248",{"doi":1329},{"id":24,"text":1332,"url":24,"identifiers":1333},"10.1128\u002Fmmbr.61.4.429-441.1997",{"doi":1332},{"id":24,"text":1335,"url":24,"identifiers":1336},"10.1111\u002Fj.1365-2672.1998.00577.x",{"doi":1335},{"id":24,"text":1338,"url":24,"identifiers":1339},"10.1128\u002Fjb.171.3.1496-1505.1989",{"doi":1338},{"id":24,"text":1341,"url":24,"identifiers":1342},"Hoover, D. 1997. Minimally processed fruits and vegetables: reducing microbial load by non-thermal physical treatments. Food Technol.51:66-71.",{},{"id":24,"text":1344,"url":24,"identifiers":1345},"Huisman G. W. D. A. Siegele M. M. Zambrano and R. Kolter. 1996. Morphological and physiological changes during stationary phase p. 1672-1682. In F. C. Neidhardt et al. (ed.) Escherichia coli and Salmonella : cellular and molecular biology. ASM Press Washington D.C.",{},{"id":24,"text":1347,"url":24,"identifiers":1348},"10.1271\u002Fbbb.63.1321",{"doi":1347},{"id":24,"text":1350,"url":24,"identifiers":1351},"10.1128\u002Fjb.151.3.1523-1531.1982",{"doi":1350},{"id":24,"text":1353,"url":24,"identifiers":1354},"Knorr, D. 1993. Effects of high-hydrostatic-pressure processes on food safety and quality. Food Technol.47:156-161.",{},{"id":24,"text":1356,"url":24,"identifiers":1357},"Ludwig H. W. Scigalla and B. Sojka. 1996. Pressure- and temperature-induced inactivation of microorganisms p. 346-363. In J. L. Markley D. B. Northrup and C. A. Royer (ed.) High pressure effects in molecular biophysics and enzymology. Oxford University Press Oxford United Kingdom.",{"doi":1358},"10.1093\u002Foso\u002F9780195097221.003.0025",{"id":24,"text":1360,"url":24,"identifiers":1361},"10.1111\u002Fj.1472-765X.1994.tb00973.x",{"doi":1360},{"id":24,"text":1363,"url":24,"identifiers":1364},"10.1128\u002FAEM.67.1.339-344.2001",{"doi":1363},{"id":24,"text":1366,"url":24,"identifiers":1367},"10.1016\u002FS0021-9258(17)37839-0",{"doi":1366},{"id":24,"text":1369,"url":24,"identifiers":1370},"10.1099\u002F13500872-145-2-419",{"doi":1369},{"id":24,"text":1372,"url":24,"identifiers":1373},"10.1128\u002FAEM.66.7.2829-2834.2000",{"doi":1372},{"id":24,"text":1375,"url":24,"identifiers":1376},"10.1128\u002FAEM.67.4.1983-1985.2001",{"doi":1375},{"id":24,"text":1378,"url":24,"identifiers":1379},"10.1046\u002Fj.1365-2621.2001.00518.x",{"doi":1378},{"id":24,"text":1381,"url":24,"identifiers":1382},"Patterson M. 1999. High-pressure treatment of foods p. 1059-1065. In R. K. Robertson A. Batt and P. D. Patel (ed.) The encyclopedia of food microbiology. Academic Press London United Kingdom.",{"doi":1383},"10.1006\u002Frwfm.1999.0815",{"id":24,"text":1385,"url":24,"identifiers":1386},"10.1016\u002FS0168-1605(00)00165-3",{"doi":1385},{"id":24,"text":1388,"url":24,"identifiers":1389},"10.1128\u002FAEM.67.10.4901-4907.2001",{"doi":1388},{"id":24,"text":1391,"url":24,"identifiers":1392},"10.1128\u002Fjb.177.13.3695-3703.1995",{"doi":1391},{"id":24,"text":1394,"url":24,"identifiers":1395},"10.1128\u002FJB.180.4.846-854.1998",{"doi":1394},{"id":24,"text":1397,"url":24,"identifiers":1398},"San Martin, M. F., G. V. Barbosa-Canovas, and B. G. Swanson. 2003. Food processing by high hydrostatic pressure. Crit. Rev. Food Sci. Nutr.42:627-645.",{},{"id":24,"text":1400,"url":24,"identifiers":1401},"10.1016\u002F0168-1605(91)90071-V",{"doi":1400},{"id":24,"text":1403,"url":24,"identifiers":1404},"10.1080\u002F08957959408201658",{"doi":1403},{"id":24,"text":1406,"url":24,"identifiers":1407},"Smelt, J. P. P. M. 1998. Recent advances in the microbiology of high pressure processing. Trends Food Sci. Technol.9:152-158.",{},{"id":24,"text":1409,"url":24,"identifiers":1410},"Sonoike K. T. Setoyama Y. Kuma and S. Kobayashi. 1992. Effect of pressure and temperature on the death rate of Lactobacillus casei and Escherichia coli p. 297-301. In C. Balny R. Hayashi K. Heremans and P. Masson (ed.) High pressure and biotechnology. Proceedings of the First European Seminar on High Pressure and Biotechnology. Colloque INSERM\u002FJohn Libbey Eurotext Ltd. Le Grande Motte France.",{},{"id":24,"text":1412,"url":24,"identifiers":1413},"10.1016\u002F0005-2736(86)90438-4",{"doi":1412},{"id":24,"text":1415,"url":24,"identifiers":1416},"10.1128\u002FAEM.68.3.1088-1095.2002",{"doi":1415},{"id":24,"text":1418,"url":24,"identifiers":1419},"10.1128\u002FAEM.64.2.509-514.1998",{"doi":1418},{"id":1421,"createTime":1422,"updateTime":1423,"relativeEntities":1424,"slug":1425,"properties":1426,"entityType":133,"verifyStatus":134,"verifyTime":1422,"verifyNote":136,"languages":1443,"translateLanguages":24,"viewCount":25,"primaryUrl":1444,"fullTextUrl":24,"authors":1445,"publicationType":210,"publisherRelationship":1516,"citationCount":25,"citationInfo":1573,"publishDate":1576,"publishYear":1574,"citationAnalyzeStatus":23,"lastCitationAnalyze":1423,"indexDatabases":1577,"openAccess":24,"references":1578,"isForceReanalyzing":408},"26916029-9cbd-4e10-803c-a8baed5ee89d","2024-09-05T04:01:25.298+00:00","2026-07-13T08:57:53.642+00:00",[],"Simple-rapid-method-for-direct-isolation-of-nucleic-acids-from-aquatic-environments",{"mag":1427,"gsPaper":1429,"pmc":1431,"openalex":1433,"abstract":1435,"title":1437,"pm":1439,"doi":1441},{"VOID":1428},"1523731348",{"VOID":1430},"[\"11696819165177903508\"]",{"VOID":1432},"184158",{"VOID":1434},"W1523731348",{"EN":1436},"\u003Cjats:p>Direct isolation of nucleic acids from the environment may be useful in several respects, including the estimation of total biomass, detection of specific organisms and genes, estimations of species diversity, and cloning applications. We have developed a method that facilitates the concentration of microorganisms from aquatic samples and the extraction of their nucleic acids. Natural water samples of 350 to greater than 1,000 ml are concentrated on a single cylindrical filter membrane (type SVGS01015; Millipore Corp., Bedford, Mass.), and cell lysis and proteolysis are carried out within the filter housing. Crude, high-molecular-weight nucleic acid solutions are then drawn off the filter. These solutions can be immediately analyzed, concentrated, or purified, depending on the intended application. The method is simple, rapid, and economical and provides high-molecular-weight chromosomal DNA, plasmid DNA, and speciated RNAs which comigrate with 5S, 16S, and 23S rRNAs. The methods presented here should prove useful in studying both the ecology and the phylogeny of microbes that resist classical culture methods.\u003C\u002Fjats:p>",{"EN":1438},"Simple, rapid method for direct isolation of nucleic acids from aquatic environments",{"VOID":1440},"2467621",{"VOID":1442},"10.1128\u002Faem.55.3.548-554.1989",[138],"https:\u002F\u002Fjournals.asm.org\u002Fdoi\u002F10.1128\u002Faem.55.3.548-554.1989",[1446,1465,1484,1501],{"id":1447,"sortIndex":25,"researcher":24,"roles":1448,"affiliations":1449,"properties":1458,"displayName":1460,"givenName":24,"familyName":24},"96985231-dff5-40a5-890d-0874e8a42f5d",[],[1450],{"id":1451,"sortIndex":25,"affiliation":1452,"properties":24},"492e89b5-4152-4442-abe1-56fdc7800a11",{"id":1451,"createTime":24,"updateTime":24,"relativeEntities":1453,"slug":24,"properties":1454,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":1457,"statistic":24},[],{"title":1455},{"EN":1456},"Center of Marine Biotechnology, University of Maryland, Baltimore 21202.",[],{"title":1459,"gsAuthor":1461,"openalex":1463},{"EN":1460},"C C Somerville",{"VOID":1462},"[\"sw3DZawAAAAJ\"]",{"VOID":1464},"A5020574668",{"id":1466,"sortIndex":160,"researcher":24,"roles":1467,"affiliations":1468,"properties":1475,"displayName":1479,"givenName":24,"familyName":24},"33546e6c-1403-4763-9d95-035ca79f1fd7",[],[1469],{"id":1451,"sortIndex":25,"affiliation":1470,"properties":24},{"id":1451,"createTime":24,"updateTime":24,"relativeEntities":1471,"slug":24,"properties":1472,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":1474,"statistic":24},[],{"title":1473},{"EN":1456},[],{"orcid":1476,"title":1478,"gsAuthor":1480,"openalex":1482},{"VOID":1477},"https:\u002F\u002Forcid.org\u002F0000-0003-2974-4065",{"EN":1479},"Ivor T. 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That inactivation is usually assessed by the number of colonies growing on solid media after treatment. Under normal conditions the method does not permit recovery of damaged cells and may underestimate the number of cells that will remain viable and grow after a few days in high-pressure-processed foodstuffs. This study investigated the damage inflicted on\n            \u003Cjats:italic>Listeria monocytogenes\u003C\u002Fjats:italic>\n            cells treated by high pressure for 10 min at 400 MPa in pH 5.6 citrate buffer. Under these conditions, no cell growth occurred after 48 h on plate count agar. Scanning electron microscopy, light scattering by flow cytometry, and cell volume measurements were compared to evaluate the morphological changes in cells after pressurization. All these methods revealed that cellular morphology was not really affected. Esterase activity, as assessed either by enzymatic activity assays or by carboxy fluorescein diacetate fluorescence monitored by flow cytometry, was dramatically lowered, but not totally obliterated, under the effects of treatment. The measurement of propidium iodide uptake followed by flow cytometry demonstrated that membrane integrity was preserved in a small part of the population, although the membrane potential measured by analytical methods or evaluated by oxonol uptake was reduced from −86 to −5 mV. These results showed that such combined methods as fluorescent dyes monitored by flow cytometry and physiological activity measurements provide valuable indications of cellular viability.\n          \u003C\u002Fjats:p>",{"EN":1596},"Morphological and Physiological Characterization of\n            \u003Ci>Listeria monocytogenes\u003C\u002Fi>\n            Subjected to High Hydrostatic Pressure",{"VOID":1598},"11319107",{"VOID":1600},"10.1128\u002Faem.67.5.2240-2247.2001","2024-08-31T20:02:19.835+00:00",[138],"https:\u002F\u002Fjournals.asm.org\u002Fdoi\u002F10.1128\u002FAEM.67.5.2240-2247.2001",[1605,1622,1639,1656],{"id":1606,"sortIndex":25,"researcher":24,"roles":1607,"affiliations":1608,"properties":1617,"displayName":1619,"givenName":24,"familyName":24},"8f6e79aa-c66d-4402-b67d-c52493185697",[],[1609],{"id":1610,"sortIndex":25,"affiliation":1611,"properties":24},"e329e69c-63fd-4489-9907-0126931353c1",{"id":1610,"createTime":24,"updateTime":24,"relativeEntities":1612,"slug":24,"properties":1613,"entityType":24,"verifyStatus":24,"verifyTime":24,"verifyNote":24,"languages":24,"translateLanguages":24,"viewCount":24,"url":24,"parentIds":1616,"statistic":24},[],{"title":1614},{"EN":1615},"Unité Mixte de Recherche, 1014 INRA\u002FENVN d'Hygiène des Aliments, Ecole Nationale Vétérinaire de Nantes, F-44307 Nantes,1",[],{"title":1618,"openalex":1620},{"EN":1619},"M. 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