Stability performance ofCynara cardunculus L. acid protease in aqueous-organic biphasic systems View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-03

AUTHORS

M. T. Barros, M. G. V. Carvalho, F. A. P. Garcia, E. M. V. Pires

ABSTRACT

Stability performance of the acid protease ofCynara cardunculus L. in biphasic systems containing ethyl acetate,n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containingn-hexane. In this system 100% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases ofn-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems. More... »

PAGES

179-184

References to SciGraph publications

  • 1987-04. Organic solvents for bioorganic synthesis in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf01023355

    DOI

    http://dx.doi.org/10.1007/bf01023355

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1039121060


    Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
    Incoming Citations Browse incoming citations for this publication using opencitations.net

    JSON-LD is the canonical representation for SciGraph data.

    TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

    [
      {
        "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
        "about": [
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Biological Sciences", 
            "type": "DefinedTerm"
          }, 
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/09", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Engineering", 
            "type": "DefinedTerm"
          }, 
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/10", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Technology", 
            "type": "DefinedTerm"
          }
        ], 
        "author": [
          {
            "affiliation": {
              "alternateName": "Centro de Biologia Celular, Universidade de Coimbra, 3000, COIMBRA, Portugal", 
              "id": "http://www.grid.ac/institutes/None", 
              "name": [
                "Centro de Biologia Celular, Universidade de Coimbra, 3000, COIMBRA, Portugal"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Barros", 
            "givenName": "M. T.", 
            "id": "sg:person.015032306170.09", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.015032306170.09"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Departamento de Engenharia Qu\u00edmica, Universidade de Coimbra, 3000, COIMBRA, Portugal", 
              "id": "http://www.grid.ac/institutes/grid.8051.c", 
              "name": [
                "Departamento de Engenharia Qu\u00edmica, Universidade de Coimbra, 3000, COIMBRA, Portugal"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Carvalho", 
            "givenName": "M. G. V.", 
            "id": "sg:person.01124112173.51", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01124112173.51"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Departamento de Engenharia Qu\u00edmica, Universidade de Coimbra, 3000, COIMBRA, Portugal", 
              "id": "http://www.grid.ac/institutes/grid.8051.c", 
              "name": [
                "Departamento de Engenharia Qu\u00edmica, Universidade de Coimbra, 3000, COIMBRA, Portugal"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Garcia", 
            "givenName": "F. A. P.", 
            "id": "sg:person.01027602120.13", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01027602120.13"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Centro de Biologia Celular, Universidade de Coimbra, 3000, COIMBRA, Portugal", 
              "id": "http://www.grid.ac/institutes/None", 
              "name": [
                "Centro de Biologia Celular, Universidade de Coimbra, 3000, COIMBRA, Portugal"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Pires", 
            "givenName": "E. M. V.", 
            "id": "sg:person.0733210265.33", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0733210265.33"
            ], 
            "type": "Person"
          }
        ], 
        "citation": [
          {
            "id": "sg:pub.10.1007/bf00282141", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1037236239", 
              "https://doi.org/10.1007/bf00282141"
            ], 
            "type": "CreativeWork"
          }
        ], 
        "datePublished": "1992-03", 
        "datePublishedReg": "1992-03-01", 
        "description": "Stability performance of the acid protease ofCynara cardunculus L. in biphasic systems containing ethyl acetate,n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containingn-hexane. In this system 100% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases ofn-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems.", 
        "genre": "article", 
        "id": "sg:pub.10.1007/bf01023355", 
        "inLanguage": "en", 
        "isAccessibleForFree": false, 
        "isPartOf": [
          {
            "id": "sg:journal.1289037", 
            "issn": [
              "0951-208X", 
              "1573-6784"
            ], 
            "name": "Biotechnology Letters", 
            "publisher": "Springer Nature", 
            "type": "Periodical"
          }, 
          {
            "issueNumber": "3", 
            "type": "PublicationIssue"
          }, 
          {
            "type": "PublicationVolume", 
            "volumeNumber": "14"
          }
        ], 
        "keywords": [
          "biphasic system", 
          "aqueous-organic biphasic system", 
          "enzyme stability", 
          "ethyl acetate", 
          "activity retention", 
          "log P", 
          "isooctane", 
          "stability", 
          "acetate", 
          "system 100", 
          "hexane", 
          "acid protease", 
          "retention", 
          "phase", 
          "stability performance", 
          "pepsin", 
          "cardunculus L.", 
          "absolute requirement", 
          "system", 
          "protease", 
          "performance", 
          "L.", 
          "results", 
          "cases", 
          "requirements", 
          "hours", 
          "acid protease ofCynara cardunculus L.", 
          "protease ofCynara cardunculus L.", 
          "ofCynara cardunculus L.", 
          "pre-saturated phases", 
          "Stability performance ofCynara cardunculus L. acid protease", 
          "performance ofCynara cardunculus L. acid protease", 
          "ofCynara cardunculus L. acid protease", 
          "cardunculus L. acid protease", 
          "L. acid protease"
        ], 
        "name": "Stability performance ofCynara cardunculus L. acid protease in aqueous-organic biphasic systems", 
        "pagination": "179-184", 
        "productId": [
          {
            "name": "dimensions_id", 
            "type": "PropertyValue", 
            "value": [
              "pub.1039121060"
            ]
          }, 
          {
            "name": "doi", 
            "type": "PropertyValue", 
            "value": [
              "10.1007/bf01023355"
            ]
          }
        ], 
        "sameAs": [
          "https://doi.org/10.1007/bf01023355", 
          "https://app.dimensions.ai/details/publication/pub.1039121060"
        ], 
        "sdDataset": "articles", 
        "sdDatePublished": "2022-01-01T18:06", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        }, 
        "sdSource": "s3://com-springernature-scigraph/baseset/20220101/entities/gbq_results/article/article_256.jsonl", 
        "type": "ScholarlyArticle", 
        "url": "https://doi.org/10.1007/bf01023355"
      }
    ]
     

    Download the RDF metadata as:  json-ld nt turtle xml License info

    HOW TO GET THIS DATA PROGRAMMATICALLY:

    JSON-LD is a popular format for linked data which is fully compatible with JSON.

    curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/bf01023355'

    N-Triples is a line-based linked data format ideal for batch operations.

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/bf01023355'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/bf01023355'

    RDF/XML is a standard XML format for linked data.

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/bf01023355'


     

    This table displays all metadata directly associated to this object as RDF triples.

    125 TRIPLES      22 PREDICATES      63 URIs      53 LITERALS      6 BLANK NODES

    Subject Predicate Object
    1 sg:pub.10.1007/bf01023355 schema:about anzsrc-for:06
    2 anzsrc-for:09
    3 anzsrc-for:10
    4 schema:author Nfafaca7800fc4933b72e4a07dbb7b56f
    5 schema:citation sg:pub.10.1007/bf00282141
    6 schema:datePublished 1992-03
    7 schema:datePublishedReg 1992-03-01
    8 schema:description Stability performance of the acid protease ofCynara cardunculus L. in biphasic systems containing ethyl acetate,n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containingn-hexane. In this system 100% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases ofn-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems.
    9 schema:genre article
    10 schema:inLanguage en
    11 schema:isAccessibleForFree false
    12 schema:isPartOf N5a953797caa94490a9b0623b4259a118
    13 N97b8dd5718bd4c8188a346b9861a1e97
    14 sg:journal.1289037
    15 schema:keywords L.
    16 L. acid protease
    17 Stability performance ofCynara cardunculus L. acid protease
    18 absolute requirement
    19 acetate
    20 acid protease
    21 acid protease ofCynara cardunculus L.
    22 activity retention
    23 aqueous-organic biphasic system
    24 biphasic system
    25 cardunculus L.
    26 cardunculus L. acid protease
    27 cases
    28 enzyme stability
    29 ethyl acetate
    30 hexane
    31 hours
    32 isooctane
    33 log P
    34 ofCynara cardunculus L.
    35 ofCynara cardunculus L. acid protease
    36 pepsin
    37 performance
    38 performance ofCynara cardunculus L. acid protease
    39 phase
    40 pre-saturated phases
    41 protease
    42 protease ofCynara cardunculus L.
    43 requirements
    44 results
    45 retention
    46 stability
    47 stability performance
    48 system
    49 system 100
    50 schema:name Stability performance ofCynara cardunculus L. acid protease in aqueous-organic biphasic systems
    51 schema:pagination 179-184
    52 schema:productId N1c1cefbc854d4faf9bd36d301ffa028d
    53 N82e4e55828fa4473b7633b39f750dd98
    54 schema:sameAs https://app.dimensions.ai/details/publication/pub.1039121060
    55 https://doi.org/10.1007/bf01023355
    56 schema:sdDatePublished 2022-01-01T18:06
    57 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    58 schema:sdPublisher Nf2739406e401406795fb16d6419f1cde
    59 schema:url https://doi.org/10.1007/bf01023355
    60 sgo:license sg:explorer/license/
    61 sgo:sdDataset articles
    62 rdf:type schema:ScholarlyArticle
    63 N0949ca1f17d848e88f289fc9e3c18312 rdf:first sg:person.01027602120.13
    64 rdf:rest N834fd681805e4775931c167e1defa655
    65 N1c1cefbc854d4faf9bd36d301ffa028d schema:name doi
    66 schema:value 10.1007/bf01023355
    67 rdf:type schema:PropertyValue
    68 N5a953797caa94490a9b0623b4259a118 schema:issueNumber 3
    69 rdf:type schema:PublicationIssue
    70 N7a4d95eb6cbc47ff9f8678142c7ce2b0 rdf:first sg:person.01124112173.51
    71 rdf:rest N0949ca1f17d848e88f289fc9e3c18312
    72 N82e4e55828fa4473b7633b39f750dd98 schema:name dimensions_id
    73 schema:value pub.1039121060
    74 rdf:type schema:PropertyValue
    75 N834fd681805e4775931c167e1defa655 rdf:first sg:person.0733210265.33
    76 rdf:rest rdf:nil
    77 N97b8dd5718bd4c8188a346b9861a1e97 schema:volumeNumber 14
    78 rdf:type schema:PublicationVolume
    79 Nf2739406e401406795fb16d6419f1cde schema:name Springer Nature - SN SciGraph project
    80 rdf:type schema:Organization
    81 Nfafaca7800fc4933b72e4a07dbb7b56f rdf:first sg:person.015032306170.09
    82 rdf:rest N7a4d95eb6cbc47ff9f8678142c7ce2b0
    83 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
    84 schema:name Biological Sciences
    85 rdf:type schema:DefinedTerm
    86 anzsrc-for:09 schema:inDefinedTermSet anzsrc-for:
    87 schema:name Engineering
    88 rdf:type schema:DefinedTerm
    89 anzsrc-for:10 schema:inDefinedTermSet anzsrc-for:
    90 schema:name Technology
    91 rdf:type schema:DefinedTerm
    92 sg:journal.1289037 schema:issn 0951-208X
    93 1573-6784
    94 schema:name Biotechnology Letters
    95 schema:publisher Springer Nature
    96 rdf:type schema:Periodical
    97 sg:person.01027602120.13 schema:affiliation grid-institutes:grid.8051.c
    98 schema:familyName Garcia
    99 schema:givenName F. A. P.
    100 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01027602120.13
    101 rdf:type schema:Person
    102 sg:person.01124112173.51 schema:affiliation grid-institutes:grid.8051.c
    103 schema:familyName Carvalho
    104 schema:givenName M. G. V.
    105 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01124112173.51
    106 rdf:type schema:Person
    107 sg:person.015032306170.09 schema:affiliation grid-institutes:None
    108 schema:familyName Barros
    109 schema:givenName M. T.
    110 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.015032306170.09
    111 rdf:type schema:Person
    112 sg:person.0733210265.33 schema:affiliation grid-institutes:None
    113 schema:familyName Pires
    114 schema:givenName E. M. V.
    115 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0733210265.33
    116 rdf:type schema:Person
    117 sg:pub.10.1007/bf00282141 schema:sameAs https://app.dimensions.ai/details/publication/pub.1037236239
    118 https://doi.org/10.1007/bf00282141
    119 rdf:type schema:CreativeWork
    120 grid-institutes:None schema:alternateName Centro de Biologia Celular, Universidade de Coimbra, 3000, COIMBRA, Portugal
    121 schema:name Centro de Biologia Celular, Universidade de Coimbra, 3000, COIMBRA, Portugal
    122 rdf:type schema:Organization
    123 grid-institutes:grid.8051.c schema:alternateName Departamento de Engenharia Química, Universidade de Coimbra, 3000, COIMBRA, Portugal
    124 schema:name Departamento de Engenharia Química, Universidade de Coimbra, 3000, COIMBRA, Portugal
    125 rdf:type schema:Organization
     




    Preview window. Press ESC to close (or click here)


    ...