arginine-to-lysine substitutions influence recombinant horseradish peroxidase stability and immobilisation effectivenessarginine-to-lysine替换影响稳定和固定辣根过氧化物酶重组效率.pdfVIP

BMC Biotechnology BioMed Central Research article Open Access Arginine-to-lysine substitutions influence recombinant horseradish peroxidase stability and immobilisation effectiveness Barry J Ryan and Ciarán ÓFágáin* Address: School of Biotechnology and National Centre for Sensors Research, Dublin City University, Dublin 9, Ireland Email: Barry J Ryan - barry.ryan5@mail.dcu.ie; Ciarán ÓFágáin* - ciaran.fagan@dcu.ie * Corresponding author Published: 5 December 2007 Received: 22 July 2007 Accepted: 5 December 2007 BMC Biotechnology 2007, 7:86 doi:10.1186/1472-6750-7-86 This article is available from: /1472-6750/7/86 © 2007 Ryan and ÓFágáin; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: Horseradish Peroxidase (HRP) plays important roles in many biotechnological fields, including diagnostics, biosensors and biocatalysis. Often, it is used in immobilised form. With conventional immobilisation techniques, the enzyme adheres in random orientation: the active site may face the solid phase rather than bulk medium, impeding substrate access and leading to sub- optimal catalytic performance. The ability to immobilise HRP in a directional manner, such that the active site would always face outwards from the insoluble matrix,