Kinetics of glucose isomerization to fructose by immobilized glucose isomerase in the presence of substrate protection View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-12

AUTHORS

A. Converti, M. Del Borghi

ABSTRACT

The activity of immobilized glucose isomerase of Streptomyces murinus has been tested batchwise under different conditions in order to gather the related kinetic parameters necessary to optimize an immobilized enzyme column for the continuous production of high fructose corn syrup (HFCS). To this purpose, the Briggs-Haldane model incorporating an apparent first-order inactivation constant has been used with success. A comparison of the equilibrium constants and of the maximum theoretical conversion yields calculated at different temperatures with those estimated for the native enzyme demonstrates that the immobilization favours the transformation of glucose to fructose only at T > 70 °C, as a possible consequence of a combined effect of catalysis and equilibrium thermodynamics enhancement. Enzyme inactivation has also been tested at different temperatures and sugar concentrations to evaluate the related kinetic parameters under different conditions of substrate protection. More... »

PAGES

27-33

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s004490050406

DOI

http://dx.doi.org/10.1007/s004490050406

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003239368


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/2008/09", 
        "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"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0903", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biomedical Engineering", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0904", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Chemical Engineering", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/1003", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Industrial Biotechnology", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Institute of Chemical and Process Engineering \u201cG.B. Bonino\u201d, Faculty of Engineering, University of Genoa, Via Opera Pia, 15, I-16145 Genoa, Italy, IT", 
          "id": "http://www.grid.ac/institutes/grid.5606.5", 
          "name": [
            "Institute of Chemical and Process Engineering \u201cG.B. Bonino\u201d, Faculty of Engineering, University of Genoa, Via Opera Pia, 15, I-16145 Genoa, Italy, IT"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Converti", 
        "givenName": "A.", 
        "id": "sg:person.0652617777.44", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0652617777.44"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Institute of Chemical and Process Engineering \u201cG.B. Bonino\u201d, Faculty of Engineering, University of Genoa, Via Opera Pia, 15, I-16145 Genoa, Italy, IT", 
          "id": "http://www.grid.ac/institutes/grid.5606.5", 
          "name": [
            "Institute of Chemical and Process Engineering \u201cG.B. Bonino\u201d, Faculty of Engineering, University of Genoa, Via Opera Pia, 15, I-16145 Genoa, Italy, IT"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Borghi", 
        "givenName": "M. Del", 
        "id": "sg:person.014000712263.71", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.014000712263.71"
        ], 
        "type": "Person"
      }
    ], 
    "datePublished": "1997-12", 
    "datePublishedReg": "1997-12-01", 
    "description": "Abstract The activity of immobilized glucose isomerase of Streptomyces murinus has been tested batchwise under different conditions in order to gather the related kinetic parameters necessary to optimize an immobilized enzyme column for the continuous production of high fructose corn syrup (HFCS). To this purpose, the Briggs-Haldane model incorporating an apparent first-order inactivation constant has been used with success. A comparison of the equilibrium constants and of the maximum theoretical conversion yields calculated at different temperatures with those estimated for the native enzyme demonstrates that the immobilization favours the transformation of glucose to fructose only at T\u2009>\u200970\u200a\u00b0C, as a possible consequence of a combined effect of catalysis and equilibrium thermodynamics enhancement. Enzyme inactivation has also been tested at different temperatures and sugar concentrations to evaluate the related kinetic parameters under different conditions of substrate protection.", 
    "genre": "article", 
    "id": "sg:pub.10.1007/s004490050406", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1297453", 
        "issn": [
          "0178-515X", 
          "1432-0797"
        ], 
        "name": "Bioprocess and Biosystems Engineering", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "1", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "18"
      }
    ], 
    "keywords": [
      "substrate protection", 
      "native enzyme", 
      "isomerase", 
      "Streptomyces murinus", 
      "glucose isomerase", 
      "inactivation", 
      "enzyme inactivation", 
      "sugar concentration", 
      "immobilized enzyme column", 
      "theoretical conversion yield", 
      "murinus", 
      "kinetic parameters", 
      "first-order inactivation", 
      "enzyme", 
      "different conditions", 
      "transformation of glucose", 
      "possible consequences", 
      "continuous production", 
      "production", 
      "conversion yield", 
      "activity", 
      "enzyme column", 
      "yield", 
      "catalysis", 
      "protection", 
      "conditions", 
      "high fructose corn syrup", 
      "glucose", 
      "consequences", 
      "presence", 
      "Abstract", 
      "success", 
      "different temperatures", 
      "transformation", 
      "effect", 
      "concentration", 
      "kinetics", 
      "isomerization", 
      "immobilized glucose isomerase", 
      "related kinetic parameters", 
      "column", 
      "comparison", 
      "temperature", 
      "immobilization", 
      "order", 
      "fructose corn syrup", 
      "corn syrup", 
      "syrup", 
      "equilibrium constants", 
      "enhancement", 
      "parameters", 
      "model", 
      "purpose", 
      "constants", 
      "effect of catalysis", 
      "thermodynamic enhancement", 
      "glucose isomerization", 
      "batchwise", 
      "Briggs\u2013Haldane model"
    ], 
    "name": "Kinetics of glucose isomerization to fructose by immobilized glucose isomerase in the presence of substrate protection", 
    "pagination": "27-33", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1003239368"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/s004490050406"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1007/s004490050406", 
      "https://app.dimensions.ai/details/publication/pub.1003239368"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-09-02T15:49", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220902/entities/gbq_results/article/article_285.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1007/s004490050406"
  }
]
 

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/s004490050406'

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/s004490050406'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/s004490050406'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s004490050406'


 

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

135 TRIPLES      20 PREDICATES      87 URIs      76 LITERALS      6 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/s004490050406 schema:about anzsrc-for:09
2 anzsrc-for:0903
3 anzsrc-for:0904
4 anzsrc-for:10
5 anzsrc-for:1003
6 schema:author N8ec3fa8ed98948258ba0b692080c4e51
7 schema:datePublished 1997-12
8 schema:datePublishedReg 1997-12-01
9 schema:description Abstract The activity of immobilized glucose isomerase of Streptomyces murinus has been tested batchwise under different conditions in order to gather the related kinetic parameters necessary to optimize an immobilized enzyme column for the continuous production of high fructose corn syrup (HFCS). To this purpose, the Briggs-Haldane model incorporating an apparent first-order inactivation constant has been used with success. A comparison of the equilibrium constants and of the maximum theoretical conversion yields calculated at different temperatures with those estimated for the native enzyme demonstrates that the immobilization favours the transformation of glucose to fructose only at T > 70 °C, as a possible consequence of a combined effect of catalysis and equilibrium thermodynamics enhancement. Enzyme inactivation has also been tested at different temperatures and sugar concentrations to evaluate the related kinetic parameters under different conditions of substrate protection.
10 schema:genre article
11 schema:isAccessibleForFree false
12 schema:isPartOf N68c396a9c8a040b09b51fe2ec9fe17a5
13 N72cdda36ae604e7c8b635ee613e75765
14 sg:journal.1297453
15 schema:keywords Abstract
16 Briggs–Haldane model
17 Streptomyces murinus
18 activity
19 batchwise
20 catalysis
21 column
22 comparison
23 concentration
24 conditions
25 consequences
26 constants
27 continuous production
28 conversion yield
29 corn syrup
30 different conditions
31 different temperatures
32 effect
33 effect of catalysis
34 enhancement
35 enzyme
36 enzyme column
37 enzyme inactivation
38 equilibrium constants
39 first-order inactivation
40 fructose corn syrup
41 glucose
42 glucose isomerase
43 glucose isomerization
44 high fructose corn syrup
45 immobilization
46 immobilized enzyme column
47 immobilized glucose isomerase
48 inactivation
49 isomerase
50 isomerization
51 kinetic parameters
52 kinetics
53 model
54 murinus
55 native enzyme
56 order
57 parameters
58 possible consequences
59 presence
60 production
61 protection
62 purpose
63 related kinetic parameters
64 substrate protection
65 success
66 sugar concentration
67 syrup
68 temperature
69 theoretical conversion yield
70 thermodynamic enhancement
71 transformation
72 transformation of glucose
73 yield
74 schema:name Kinetics of glucose isomerization to fructose by immobilized glucose isomerase in the presence of substrate protection
75 schema:pagination 27-33
76 schema:productId N11f66d5082e347aaaf7da291a6d00264
77 N644d8b8441734607aeac335681d526f3
78 schema:sameAs https://app.dimensions.ai/details/publication/pub.1003239368
79 https://doi.org/10.1007/s004490050406
80 schema:sdDatePublished 2022-09-02T15:49
81 schema:sdLicense https://scigraph.springernature.com/explorer/license/
82 schema:sdPublisher N220d4fd400fa411ba93a974b60782034
83 schema:url https://doi.org/10.1007/s004490050406
84 sgo:license sg:explorer/license/
85 sgo:sdDataset articles
86 rdf:type schema:ScholarlyArticle
87 N11f66d5082e347aaaf7da291a6d00264 schema:name doi
88 schema:value 10.1007/s004490050406
89 rdf:type schema:PropertyValue
90 N220d4fd400fa411ba93a974b60782034 schema:name Springer Nature - SN SciGraph project
91 rdf:type schema:Organization
92 N60934ace3f474418ba3fc59e6715ca70 rdf:first sg:person.014000712263.71
93 rdf:rest rdf:nil
94 N644d8b8441734607aeac335681d526f3 schema:name dimensions_id
95 schema:value pub.1003239368
96 rdf:type schema:PropertyValue
97 N68c396a9c8a040b09b51fe2ec9fe17a5 schema:issueNumber 1
98 rdf:type schema:PublicationIssue
99 N72cdda36ae604e7c8b635ee613e75765 schema:volumeNumber 18
100 rdf:type schema:PublicationVolume
101 N8ec3fa8ed98948258ba0b692080c4e51 rdf:first sg:person.0652617777.44
102 rdf:rest N60934ace3f474418ba3fc59e6715ca70
103 anzsrc-for:09 schema:inDefinedTermSet anzsrc-for:
104 schema:name Engineering
105 rdf:type schema:DefinedTerm
106 anzsrc-for:0903 schema:inDefinedTermSet anzsrc-for:
107 schema:name Biomedical Engineering
108 rdf:type schema:DefinedTerm
109 anzsrc-for:0904 schema:inDefinedTermSet anzsrc-for:
110 schema:name Chemical Engineering
111 rdf:type schema:DefinedTerm
112 anzsrc-for:10 schema:inDefinedTermSet anzsrc-for:
113 schema:name Technology
114 rdf:type schema:DefinedTerm
115 anzsrc-for:1003 schema:inDefinedTermSet anzsrc-for:
116 schema:name Industrial Biotechnology
117 rdf:type schema:DefinedTerm
118 sg:journal.1297453 schema:issn 0178-515X
119 1432-0797
120 schema:name Bioprocess and Biosystems Engineering
121 schema:publisher Springer Nature
122 rdf:type schema:Periodical
123 sg:person.014000712263.71 schema:affiliation grid-institutes:grid.5606.5
124 schema:familyName Borghi
125 schema:givenName M. Del
126 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.014000712263.71
127 rdf:type schema:Person
128 sg:person.0652617777.44 schema:affiliation grid-institutes:grid.5606.5
129 schema:familyName Converti
130 schema:givenName A.
131 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0652617777.44
132 rdf:type schema:Person
133 grid-institutes:grid.5606.5 schema:alternateName Institute of Chemical and Process Engineering “G.B. Bonino”, Faculty of Engineering, University of Genoa, Via Opera Pia, 15, I-16145 Genoa, Italy, IT
134 schema:name Institute of Chemical and Process Engineering “G.B. Bonino”, Faculty of Engineering, University of Genoa, Via Opera Pia, 15, I-16145 Genoa, Italy, IT
135 rdf:type schema:Organization
 




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


...