Reference : Modification of the Thermoresistance to Spray-Drying of a Cold-Adapted Subtilisin by ...
Scientific journals : Article
Life sciences : Biotechnology
Life sciences : Microbiology
http://hdl.handle.net/2268/25925
Modification of the Thermoresistance to Spray-Drying of a Cold-Adapted Subtilisin by Genetic Engineering
English
Bare, G. [> > > >]
Diakiese, A. [> > > >]
Zgoulli, S. [> > > >]
Sabri, Ahmed mailto [Université de Liège - ULg > > Centre Wallon de biologie industrielle >]
Gerday, Charles mailto [Université de Liège - ULg > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Thonart, Philippe mailto [Université de Liège - ULg > Département des sciences de la vie > Biochimie et microbiologie industrielles >]
1999
Applied Biochemistry and Biotechnology
77-79
Spring
857-65
Yes (verified by ORBi)
International
0273-2289
[en] Subtilisin ; mutations ; cold-adapted enzyme ; thermoresistance ; spray-drying
[en] The thermoresistance of a cold-adapted subtilisin dried by spray-drying was studied. Proteolytic activity of this enzyme was measured before and after spray-drying. Without chemical additives, spray-drying yields ranged from 2-13%. The use of arabic gum and lactose in the composition of the enzyme solutions allowed the strengthening of the enzyme structures and increased water mobility in the product. Increase of water mobility led to a shorter residence time of the product in the spray-drier and a net yield increase was obtained (yield higher than 50%). The effect of two selective mutations on the thermoresistance to spray-drying of the cold-adapted subtilisin was also investigated. Mutation T85D (introduction of an additional link with an ion Ca2+ necessary for enzyme activity, by substitution of Asp for Thr 85) had no effect on the thermoresistance of the subtilisin to spray-drying. Mutation H121W (introduction of an additional aromatic link by substitution of Trp for His 121) reduced the drying yield from 66% (not modified subtilisin) to 52%. This higher thermosensitivity could be explained by an increase of the hygroscopic character of the modified subtilisin (mutation H121W).
http://hdl.handle.net/2268/25925

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