View in EDS PDF Full Text

Novel immobilization process of a thermophilic catalase: efficient purification by heat treatment and subsequent immobilization at high temperature.

Saved in:
Bibliographic Details
Title: Novel immobilization process of a thermophilic catalase: efficient purification by heat treatment and subsequent immobilization at high temperature.
Authors: Xu, Juan, Luo, Hui1 luohui@ustb.edu.cn, López, Claudia, Xiao, Jing, Chang, Yanhong yhchang@ustb.edu.cn
Source: Bioprocess & Biosystems Engineering. Oct2015, Vol. 38 Issue 10, p1983-1991. 9p.
Subjects: Catalase, Heat treatment, Therapeutic immobilization, High temperatures, Thermal stability
Abstract: The main goal of the present work is to investigate a novel process of purification and immobilization of a thermophilic catalase at high temperatures. The catalase, originated from Bacillus sp., was overexpressed in a recombinant Escherichia coli BL21(DE3)/pET28-CATHis and efficiently purified by heat treatment, achieving a threefold purification. The purified catalase was then immobilized onto an epoxy support at different temperatures (25, 40, and 55 °C). The immobilizate obtained at higher temperatures reached its maximum activity in a shorter time than that obtained at lower temperatures. Furthermore, immobilization at higher temperatures required a lower ionic strength than immobilization at lower temperatures. The characteristics of immobilized enzymes prepared at different temperatures were investigated. The high-temperature immobilizate (55 °C) showed the highest thermal stability, followed by the 40 °C immobilizate. And the high-temperature immobilizate (55 °C) had slightly higher operational stability than the 25 °C immobilizate. All of the immobilized catalase preparations showed higher stability than the free enzyme at alkaline pH 10.0, while the alkali resistance of the 25 °C immobilizate was slightly better than that of the 40 and 55 °C immobilizates. [ABSTRACT FROM AUTHOR]
Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Links:
  – Type: pdflink
Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 109927508
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Novel immobilization process of a thermophilic catalase: efficient purification by heat treatment and subsequent immobilization at high temperature.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Xu%2C+Juan%22">Xu, Juan</searchLink><br /><searchLink fieldCode="AR" term="%22Luo%2C+Hui%22">Luo, Hui</searchLink><relatesTo>1</relatesTo><i> luohui@ustb.edu.cn</i><br /><searchLink fieldCode="AR" term="%22López%2C+Claudia%22">López, Claudia</searchLink><br /><searchLink fieldCode="AR" term="%22Xiao%2C+Jing%22">Xiao, Jing</searchLink><br /><searchLink fieldCode="AR" term="%22Chang%2C+Yanhong%22">Chang, Yanhong</searchLink><i> yhchang@ustb.edu.cn</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Bioprocess+%26+Biosystems+Engineering%22">Bioprocess & Biosystems Engineering</searchLink>. Oct2015, Vol. 38 Issue 10, p1983-1991. 9p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Catalase%22">Catalase</searchLink><br /><searchLink fieldCode="DE" term="%22Heat+treatment%22">Heat treatment</searchLink><br /><searchLink fieldCode="DE" term="%22Therapeutic+immobilization%22">Therapeutic immobilization</searchLink><br /><searchLink fieldCode="DE" term="%22High+temperatures%22">High temperatures</searchLink><br /><searchLink fieldCode="DE" term="%22Thermal+stability%22">Thermal stability</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The main goal of the present work is to investigate a novel process of purification and immobilization of a thermophilic catalase at high temperatures. The catalase, originated from Bacillus sp., was overexpressed in a recombinant Escherichia coli BL21(DE3)/pET28-CATHis and efficiently purified by heat treatment, achieving a threefold purification. The purified catalase was then immobilized onto an epoxy support at different temperatures (25, 40, and 55 °C). The immobilizate obtained at higher temperatures reached its maximum activity in a shorter time than that obtained at lower temperatures. Furthermore, immobilization at higher temperatures required a lower ionic strength than immobilization at lower temperatures. The characteristics of immobilized enzymes prepared at different temperatures were investigated. The high-temperature immobilizate (55 °C) showed the highest thermal stability, followed by the 40 °C immobilizate. And the high-temperature immobilizate (55 °C) had slightly higher operational stability than the 25 °C immobilizate. All of the immobilized catalase preparations showed higher stability than the free enzyme at alkaline pH 10.0, while the alkali resistance of the 25 °C immobilizate was slightly better than that of the 40 and 55 °C immobilizates. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=109927508
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1007/s00449-015-1439-y
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 9
        StartPage: 1983
    Subjects:
      – SubjectFull: Catalase
        Type: general
      – SubjectFull: Heat treatment
        Type: general
      – SubjectFull: Therapeutic immobilization
        Type: general
      – SubjectFull: High temperatures
        Type: general
      – SubjectFull: Thermal stability
        Type: general
    Titles:
      – TitleFull: Novel immobilization process of a thermophilic catalase: efficient purification by heat treatment and subsequent immobilization at high temperature.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Xu, Juan
      – PersonEntity:
          Name:
            NameFull: Luo, Hui
      – PersonEntity:
          Name:
            NameFull: López, Claudia
      – PersonEntity:
          Name:
            NameFull: Xiao, Jing
      – PersonEntity:
          Name:
            NameFull: Chang, Yanhong
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 10
              Text: Oct2015
              Type: published
              Y: 2015
          Identifiers:
            – Type: issn-print
              Value: 16157591
          Numbering:
            – Type: volume
              Value: 38
            – Type: issue
              Value: 10
          Titles:
            – TitleFull: Bioprocess & Biosystems Engineering
              Type: main
ResultId 1