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Cell disruption optimization and covalent immobilization of beta-D-galactosidase from kluyveromyces marxianus YW-1 for lactose hydrolysis in milk

Puri, Munish, Gupta, Shivani, Pahuja, Parveen, Kaur, Aneet, Kanwar, J. R. and Kennedy, J. F. 2010, Cell disruption optimization and covalent immobilization of beta-D-galactosidase from kluyveromyces marxianus YW-1 for lactose hydrolysis in milk, Applied biochemistry and biotechnology, vol. 160, pp. 98-108.

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Title Cell disruption optimization and covalent immobilization of beta-D-galactosidase from kluyveromyces marxianus YW-1 for lactose hydrolysis in milk
Formatted title Cell disruption optimization and covalent immobilization of beta-D-galactosidase from kluyveromyces marxianus YW-1 for lactose hydrolysis in milk
Author(s) Puri, Munish
Gupta, Shivani
Pahuja, Parveen
Kaur, Aneet
Kanwar, J. R.
Kennedy, J. F.
Journal name Applied biochemistry and biotechnology
Volume number 160
Start page 98
End page 108
Total pages 11
Publisher Humana Press
Place of publication Totowa, United States
Publication date 2010
ISSN 0273-2289
1559-0291
Keyword(s) galactosidase
cell disruption
wheat Bran
immobilization
lactose hydrolysis
Summary β-D-galactosidase (EC 3.2.1.23) from Kluyveromyces marxianus YW-1, an isolate from whey, has been studied in terms of cell disruption to liberate the useful enzyme. The enzyme produced in a bioreactor on a wheat bran medium has been successfully immobilized with a view to developing a commercially usable technology for lactose hydrolysis in the food industry. Three chemical and three physical methods of cell disruption were tested and a method of grinding with river sand was found to give highest enzyme activity (720 U). The enzyme was covalently immobilized on gelatin. Immobilized enzyme had optimum pH and temperature of 7.0 and 40 °C, respectively and was found to give 49% hydrolysis of lactose in milk after 4 h of incubation. The immobilized enzyme was used for eight hydrolysis batches without appreciable loss in activity. The retention of high catalytic activity compared with the losses experienced with several previously reported immobilized versions of the enzyme is significant. The method of immobilization is simple, effective, and can be used for the immobilization of other enzymes.
Notes Published online: 7 February 2009
Language eng
Field of Research 060107 Enzymes
100302 Bioprocessing, Bioproduction and Bioproducts
HERDC Research category C1 Refereed article in a scholarly journal
HERDC collection year 2010
Copyright notice ©2009, Humana Press
Persistent URL http://hdl.handle.net/10536/DRO/DU:30019693

Document type: Journal Article
Collection: Centre for Biotechnology and Interdisciplinary Sciences (BioDeakin)
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Citation counts: TR Web of Science Citation Count  Cited 13 times in TR Web of Science
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Created: Fri, 18 Sep 2009, 15:04:29 EST by Munish Puri