37
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities

      research-article
      1 , 1 , 1 ,
      Chemistry Central Journal
      BioMed Central

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Background

          The use of immobilized enzymes for catalyzing various biotransformations is now a widely used approach. In recent years, cross-linked enzyme aggregates (CLEAs) have emerged as a novel and versatile biocatalyst design. The present work deals with the preparation of a CLEA from a commercial preparation, Pectinex™ Ultra SP-L, which contains pectinase, xylanase and cellulase activities. The CLEA obtained could be used for any of the enzyme activities. The CLEA was characterized in terms of kinetic parameters, thermal stability and reusability in the context of all the three enzyme activities.

          Results

          Complete precipitation of the three enzyme activities was obtained with n-propanol. When resulting precipitates were subjected to cross-linking with 5 mM glutaraldehyde, the three activities initially present (pectinase, xylanase and cellulase) were completely retained after cross-linking. The V max/K m values were increased from 11, 75 and 16 to 14, 80 and 19 in case of pectinase, xylanase and cellulase activities respectively. The thermal stability was studied at 50°C, 60°C and 70°C for pectinase, xylanase and cellulase respectively. Half-lives were improved from 17, 22 and 32 minutes to 180, 82 and 91 minutes for pectinase, xylanase and cellulase respectively. All three of the enzymes in CLEA could be reused three times without any loss of activity.

          Conclusion

          A single multipurpose biocatalyst has been designed which can be used for carrying out three different and independent reactions; 1) hydrolysis of pectin, 2) hydrolysis of xylan and 3) hydrolysis of cellulose. The preparation is more stable at higher temperatures as compared to the free enzymes.

          Related collections

          Most cited references27

          • Record: found
          • Abstract: not found
          • Article: not found

          Measurement of cellulase activities

          T. Ghose (1987)
            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found

            Interlaboratory testing of methods for assay of xylanase activity

              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs).

              The broad applicability of the cross-linking of enzyme aggregates to the effective immobilisation of enzymes is demonstrated and the influence of many parameters on the properties of the resulting CLEAs is determined. The relative simplicity of the operation ideally lends itself to high-throughput methodologies. The aggregation method was improved up to 100% activity yield for any enzyme. For the first time, the physical structures of CLEAs are elucidated. Copyright 2004 Wiley Periodicals, Inc.
                Bookmark

                Author and article information

                Journal
                Chem Cent J
                Chemistry Central Journal
                BioMed Central (London )
                1752-153X
                2007
                8 June 2007
                : 1
                : 16
                Affiliations
                [1 ]Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India
                Article
                1752-153X-1-16
                10.1186/1752-153X-1-16
                1994061
                17880745
                b5060967-cfa6-4b94-bce8-4e0c7880622e
                Copyright © 2007 Dalal et al; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 10 April 2007
                : 8 June 2007
                Categories
                Research Article

                Chemistry
                Chemistry

                Comments

                Comment on this article