Partial Purification and Immobilization/Stabilization on Highly Activated Glyoxyl-agarose Supports of Different Proteases from Flavourzyme

详细信息    查看全文

• 作者：Mar&iacute ; a del Mar Yust ; Justo Pedroche ; Manuel Alaiz ; Julio Giró ; n-Calle ; Javier Vioque ; Cé ; sar Mateo ; José ; Manuel Guisá ; n ; Francisco Millá ; n ; Roberto Fernandez-Lafuen
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2007
• 出版时间：August 8, 2007
• 年：2007
• 卷：55
• 期：16
• 页码：6503 - 6508
• 全文大小：112K
• 年卷期：v.55,no.16(August 8, 2007)
• ISSN：1520-5118

文摘

The fractioning of some components and their immobilization of Flavourzyme, a commercial protease/aminopeptidase preparation, has been investigated to improve its specificity and stability. Adsorptionof Flavourzyme on two ionic exchangers yielded two fractions with endoprotease activity and onefraction containing aminopeptidase activity. The use of an amine agarose gel has made it possibleto purify a 43 kDa protein with only endoprotease activity. Immobilization of this endoprotease andthe original Flavourzyme preparation onto glyoxyl-agarose provided derivatives that were morethermostable than their soluble counterparts. Tests using immobilized Flavourzyme and immobilizedpurified endoprotease for the hydrolysis of chickpea proteins showed that both preparations can beused for the production of protein hydrolysates and compare very favorably with the original crudeFlavourzyme in terms of reducing the production of free amino acids. This was especially so in thecase of immobilized endoprotease, which produced only 0.2% free amino acids. Keeping free aminoacids content low is very important in protein hydrolysates for nutritional use to avoid excessive osmoticpressure.