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Crosslinking of glucoamylases via carbohydrates hardly affects catalysis but impairs stability

1999; Wiley; Volume: 63; Issue: 4 Linguagem: Inglês

10.1002/(sici)1097-0290(19990520)63

1097-0290

Zsuzsanna Sasvári, Bence Asbóth,

Protein Hydrolysis and Bioactive Peptides

Biotechnology and BioengineeringVolume 63, Issue 4 p. 459-463 Crosslinking of glucoamylases via carbohydrates hardly affects catalysis but impairs stability Zsuzsanna Sasvári, Corresponding Author Zsuzsanna Sasvári Sasvari@hubi.abc.hu Agricultural Biotechnology Center, Szent-Györgyi A. u. 4, H-2100 Gödöllö, HungaryAgricultural Biotechnology Center, Szent-Györgyi A. u. 4, H-2100 Gödöllö, HungarySearch for more papers by this authorBence Asbóth, Bence Asbóth Agricultural Biotechnology Center, Szent-Györgyi A. u. 4, H-2100 Gödöllö, HungarySearch for more papers by this author Zsuzsanna Sasvári, Corresponding Author Zsuzsanna Sasvári Sasvari@hubi.abc.hu Agricultural Biotechnology Center, Szent-Györgyi A. u. 4, H-2100 Gödöllö, HungaryAgricultural Biotechnology Center, Szent-Györgyi A. u. 4, H-2100 Gödöllö, HungarySearch for more papers by this authorBence Asbóth, Bence Asbóth Agricultural Biotechnology Center, Szent-Györgyi A. u. 4, H-2100 Gödöllö, HungarySearch for more papers by this author First published: 26 March 2000 https://doi.org/10.1002/(SICI)1097-0290(19990520)63:4 3.0.CO;2-ICitations: 8AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Mild oxidation of glucoamylases from Aspergillus niger (E.C.3.2.1.3.) with periodate, followed by incubation with adipic acid dihydrazide, covalently linked enzyme molecules via their glycosyl groups. Size exclusion chromatography demonstrated and electron microscopy confirmed the formation of tetramers and octamers. Heat inactivation studies in the range of 60° to 80°C indicated that, in contrast to a priori expectations, crosslinking via the carbohydrates decreased rather than increased thermostability. The covalently linked species, even the octamers, displayed similar activity as the native forms toward maltose and soluble starch, but activity toward raw starch was completely lost. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 63: 459–463, 1999. Citing Literature Volume63, Issue420 May 1999Pages 459-463 RelatedInformation