Academic Journal

Effects of phthalic anhydride modification on horseradish peroxidase stability and activity

التفاصيل البيبلوغرافية
العنوان: Effects of phthalic anhydride modification on horseradish peroxidase stability and activity
المؤلفون: O'Brien, Anne Marie, Smith, Andrew T., Ó'Fágáin, Ciarán
المساهمون: British Council, Dublin City University, European Commission 4th Framework Biotechnology Programme
المصدر: Biotechnology and Bioengineering ; volume 81, issue 2, page 233-240 ; ISSN 0006-3592 1097-0290
بيانات النشر: Wiley
سنة النشر: 2002
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: Phthalic anhydride (PA) modification stabilizes horseradish peroxidase (HRP) by reversal of the positive charge on two of HRP's six lysine residues. Native and PA‐HRP had half‐inactivation temperatures of 51 and 65°C and half‐lives at 65°C of 4 and 17 min, respectively. PA‐HRP was more resistant to dimethylformamide at room temperature and tetrahydrofuran at 60°C and to unfolding by heat, guanidine chloride, EDTA, and the reducing agent tris(2‐carboxyethyl)phosphine hydrochloride. Binding of the hydrophobic probe Nile Red to the native enzyme and to PA‐HRP was similar. The kinetics of both HRPs with the substrates ABTS, ferrocyanide, ferulic acid, and indole‐3‐propionic acid were measured, as was binding of the inhibitor benzhydroxamic acid. Small improvements in the catalytic properties were detected. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 81: 233–240, 2003.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1002/bit.10462
الاتاحة: http://dx.doi.org/10.1002/bit.10462
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbit.10462
https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.10462
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رقم الانضمام: edsbas.F534CB67
قاعدة البيانات: BASE