Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/1944

TitleChemical modifications on proteins using glutaraldehyde
Author(s)Silva, Carla J. S. M.
Sousa, Fernanda
Gübitz, Georg M.
Paulo, Artur Cavaco
Keywordschromatography
protease
proteins
crosslinking
glutaraldehyde
SDS-PAGE
Issue date2004
PublisherUniversity of Zagreb. Faculty of Textile Technology
JournalFood Technology and Biotechnology
Citation"Food technology and biotechnology". ISSN 1330-9862. 42 (1) (2004) 51-56.
Abstract(s)In this work the effect of crosslinking the enzyme esperase (E.C. 3.4.21.62) and the proteins bovine serum albumin and casein with the bifunctional compound glutaraldehyde on molecular mass increase was studied. Two common techniques for measuring molecular mass of proteins were used: SEC and SDS-PAGE. These techniques revealed that the proteins bovine albumin and casein, when subjected to chemical crosslinking with glutaraldehyde, volume fraction 0.25%, increased their molecular mass by 20- and 40-fold, respectively. It was also observed that M-r increased proportionally to the increase of glutaraldehyde concentration in the solution, and that the addition of glutaraldehyde should be done slowly, in small amounts, in order to attain bigger protein aggregates. When the proteolytic enzyme esperase was subjected to glutaraldehyde, no increase in its M-r was achieved. Several assumptions can be made to explain these results, the most reasonable being the low amount of free lysine groups available for crosslinking. This study confirms that glutaraldehyde is not an adequate crosslinker for esperase.
TypeArticle
URIhttp://hdl.handle.net/1822/1944
ISSN1330-9862
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DET/2C2T - Artigos em revistas internacionais com arbitragem científica

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