{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670320347262080.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1128/jb.138.3.663-670.1979"}},{"identifier":{"@type":"URI","@value":"https://journals.asm.org/doi/pdf/10.1128/jb.138.3.663-670.1979"}}],"dc:title":[{"@value":"Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>Among 21 different polysaccharides tested, 5 greatly enhanced the spontaneous and cyclic AMP-induced formation of exolipase: glycogen, hyaluronate, laminarin, pectin B, and gum arabic. These polysaccharides have in common the tendency to form highly ordered networks because of the branching or helical arrangement, or both, of their molecules. None of the polysaccharides could be utilized by the cells as the sole carbon source. Strong lipid extraction of four different polysaccharides did not reduce their exolipase-enhancing efficacy. At a constant cell density the stimulation of exolipase formation by various concentrations of glycogen followed saturation kinetics, suggesting a limited number of \"sites\" for the glycogen to act. The active principle present in a solution of pectin was destroyed by degradation (beta-elimination) of the polymer. Hyaluronate lost its exolipase-enhancing activity by exhaustive hydrolysis with hyaluronidase but was resistant to proteinase K. Exopolysaccharide, isolated from growth medium of Serratia marcescens SM-6, enhanced the exolipase formation as efficiently as hyaluronate. The results of this work are discussed mainly in terms of the \"detachment hypothesis.\"</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380021390768957573","@type":"Researcher","foaf:name":[{"@value":"U K Winkler"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320347262080","@type":"Researcher","foaf:name":[{"@value":"M Stuckmann"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219193"},{"@type":"EISSN","@value":"10985530"},{"@type":"PISSN","@value":"https://id.crossref.org/issn/00219193"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/00219193"}],"prism:publicationName":[{"@value":"Journal of Bacteriology"}],"dc:publisher":[{"@value":"American Society for Microbiology"}],"prism:publicationDate":"1979-06","prism:volume":"138","prism:number":"3","prism:startingPage":"663","prism:endingPage":"670"},"reviewed":"false","dc:rights":["https://journals.asm.org/non-commercial-tdm-license"],"url":[{"@id":"https://journals.asm.org/doi/pdf/10.1128/jb.138.3.663-670.1979"}],"createdAt":"2020-01-03","modifiedAt":"2021-07-29","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360021390768957440","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Exploring the Interplay between Nutrients, Bacteriophages, and Bacterial Lipases in Host- and Bacteria-mediated Pathogenesis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360567181456090496","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Characterization of a New Cold-adapted Lipase from Pseudomonas sp. TK-3"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204090979968","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Purification and Physicochemical Properties of Lipase from Thermophilic <i>Bacillus aerius</i>"},{"@value":"Purification and Physicochemical Properties of Lipase from Thermophilic Bacillus aerius"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204091463040","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Characterization and Catalytic Properties of Free and Silica-Bound Lipase: a Comparative Study"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204093092096","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Comparative Study of Free and Immobilized Lipase from <i>Bacillus aerius</i> and its Application in Synthesis of Ethyl Ferulate"},{"@value":"Comparative Study of Free and Immobilized Lipase from Bacillus aerius and its Application in Synthesis of Ethyl Ferulate"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204146467328","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Studies on the enhanced production of extracellular lipase by Staphylococcus epidermidis"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206476364544","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Gene Cloning and Characterization of Thermostable Lipase from Bacillus stearothermophilus L1."},{"@language":"ja-Kana","@value":"Gene Cloning and Characterization of Th"},{"@value":"Gene Cloning and Characterization of Thermostable Lipase from<i>Bacillus stearothermophilus</i>L1"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679068853632","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Immobilization of Lipase from <i>Geobacillus</i> sp. and Its Application in Synthesis of Methyl Salicylate"},{"@value":"Immobilization of Lipase from Geobacillus sp. and Its Application in Synthesis of Methyl Salicylate"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679544920064","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Biodiesel Production from Crude Sunflower Oil and Crude Jatropha Oil Using Immobilized Lipase"}]},{"@id":"https://cir.nii.ac.jp/crid/1390303697454999680","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Extracellular enzymatic activity profiles in fungi isolated from oil-rich environments"}]},{"@id":"https://cir.nii.ac.jp/crid/1390565134813873664","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Application of Lipase Purified from <i>Aspergillus fumigatus</i> in the Syntheses of Ethyl Acetate and Ethyl Lactate"},{"@value":"Application of Lipase Purified from Aspergillus fumigatus in the Syntheses of Ethyl Acetate and Ethyl Lactate"}]},{"@id":"https://cir.nii.ac.jp/crid/1390845702295567360","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Synthesis of Methyl Butyrate Catalyzed by Lipase from <i>Asper</i><i>gillus fumigatus</i>"},{"@value":"Synthesis of Methyl Butyrate Catalyzed by Lipase from Aspergillus fumigatus"}]},{"@id":"https://cir.nii.ac.jp/crid/1520291855228725888","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Symbiotic effects of a lipase-secreting bacterium, Burkholderia arboris SL1B1, and a glycerol-assimilating yeast, Candida cylindracea SL1B2, on triacylglycerol degradation"},{"@language":"ja-Kana","@value":"Symbiotic effects of a lipase secreting bacterium Burkholderia arboris SL1B1 and a glycerol assimilating yeast Candida cylindracea SL1B2 on triacylglycerol degradation"}]},{"@id":"https://cir.nii.ac.jp/crid/1520573330116976896","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Optimization of cultural conditions for biosurfactant production by Pleurotus djamor in solid state fermentation"}]},{"@id":"https://cir.nii.ac.jp/crid/1521136280423917568","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Production and Stabilization of a Solvent-Tolerant Alkaline Lipase from Pseudomonas pseudoalcaligenes F-111"},{"@language":"ja-Kana","@value":"Production and Stabilization of a Solvent-Tolerant Alkaline Lipase from Pseudomonas pseudoalcaligenes F-111"}]},{"@id":"https://cir.nii.ac.jp/crid/1521980705548057856","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Production and Immobilization of Lipase from Aeromonas sobria Harboring a Heterologous Gene"},{"@language":"ja-Kana","@value":"Production and Immobilization of Lipase"}]},{"@id":"https://cir.nii.ac.jp/crid/1523669554860073216","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Functional analysis of FarA transcription factor in the regulation of the genes encoding lipolytic enzymes and hydrophobic surface binding protein for the degradation of biodegradable plastics in Aspergillus oryzae"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1128/jb.138.3.663-670.1979"},{"@type":"CROSSREF","@value":"10.1016/j.jbiosc.2011.12.014_references_DOI_RlQuPjyylTy7q6rbvQptzvWJA6A"},{"@type":"CROSSREF","@value":"10.2174/0118715303257321231024094904_references_DOI_RlQuPjyylTy7q6rbvQptzvWJA6A"},{"@type":"CROSSREF","@value":"10.1271/bbb.62.66_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.5650/jos.ess14094_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.2323/jgam.52.315_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.1007/s10267-004-0221-9_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.1007/s12010-012-9776-7_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.5650/jos.ess13231_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.5650/jos.ess14026_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.5650/jos.ess16153_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.1252/jcej.09we010_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.5650/jos.ess19202_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.1016/j.jbiosc.2015.03.007_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.1016/j.jbiosc.2008.12.001_references_DOI_RlQuPjyylTy7q6rbvQptzvWJA6A"},{"@type":"CROSSREF","@value":"10.1016/s0922-338x(98)80140-2_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.1016/s0922-338x(97)86981-4_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"},{"@type":"CROSSREF","@value":"10.5650/jos.ess19125_references_DOI_36aQTMpVetJK4VHRhJEGq9WKBYT"}]}