Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Covalent Immobilization
المؤلفون المشاركون
Branco, Roberta Vieira
Freire, Denise Maria Guimarães
Palomo, Jose Miguel
Guisan, Jose M.
Estrada Gutarra, Melissa Limoeiro
Almeida, Rodrigo Volcan
المصدر
العدد
المجلد 2015، العدد 2015 (31 ديسمبر/كانون الأول 2015)، ص ص. 1-8، 8ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2015-03-08
دولة النشر
مصر
عدد الصفحات
8
التخصصات الرئيسية
الملخص EN
A recombinant thermostable lipase (Pf2001Δ60) from the hyperthermophilic Archaeon Pyrococcus furiosus (PFUL) was immobilized by hydrophobic interaction on octyl-agarose (octyl PFUL) and by covalent bond on aldehyde activated-agarose in the presence of DTT at pH = 7.0 (one-point covalent attachment) (glyoxyl-DTT PFUL) and on glyoxyl-agarose at pH 10.2 (multipoint covalent attachment) (glyoxyl PFUL).
The enzyme’s properties, such as optimal temperature and pH, thermostability, and selectivity, were improved by covalent immobilization.
The highest enzyme stability at 70°C for 48 h incubation was achieved for glyoxyl PFUL (around 82% of residual activity), whereas glyoxyl-DTT PFUL maintained around 69% activity, followed by octyl PFUL (27% remaining activity).
Immobilization on glyoxyl-agarose improved the optimal temperature to 90°C, while the optimal temperature of octyl PFUL was 70°C.
Also, very significant changes in activity with different substrates were found.
In general, the covalent bond derivatives were more active than octyl PFUL.
The E value also depended substantially on the derivative and the conditions used.
It was observed that the reaction of glyoxyl-DTT PFUL using methyl mandelate as a substrate at pH 7 presented the best results for enantioselectivity E = 22 and enantiomeric excess (ee (%) = 91).
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
Branco, Roberta Vieira& Estrada Gutarra, Melissa Limoeiro& Guisan, Jose M.& Freire, Denise Maria Guimarães& Almeida, Rodrigo Volcan& Palomo, Jose Miguel. 2015. Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Covalent Immobilization. BioMed Research International،Vol. 2015, no. 2015, pp.1-8.
https://search.emarefa.net/detail/BIM-1054754
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
Branco, Roberta Vieira…[et al.]. Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Covalent Immobilization. BioMed Research International No. 2015 (2015), pp.1-8.
https://search.emarefa.net/detail/BIM-1054754
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
Branco, Roberta Vieira& Estrada Gutarra, Melissa Limoeiro& Guisan, Jose M.& Freire, Denise Maria Guimarães& Almeida, Rodrigo Volcan& Palomo, Jose Miguel. Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Covalent Immobilization. BioMed Research International. 2015. Vol. 2015, no. 2015, pp.1-8.
https://search.emarefa.net/detail/BIM-1054754
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-1054754
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
تقوم هذه الخدمة بالتحقق من التشابه أو الانتحال في الأبحاث والمقالات العلمية والأطروحات الجامعية والكتب والأبحاث باللغة العربية، وتحديد درجة التشابه أو أصالة الأعمال البحثية وحماية ملكيتها الفكرية. تعرف اكثر