کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8328139 | 1540205 | 2018 | 32 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Catalytic activation of Bacillus laccase after temperature treatment: Structural & biochemical characterization
ترجمه فارسی عنوان
فعال شدن کاتالیزوری لاکتوز باسیلوس پس از درمان درجه حرارت: مشخصات ساختاری و بیوشیمیایی
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
چکیده انگلیسی
Laccases belong to a family of multicopper oxidases that have strong oxidation ability towards phenolic compounds. Here, more detailed investigations were carried out on a Bacillus laccase with remarkable behavior of activation after thermal treatment. The kcat of the enzyme was increased 2.5 fold after 50â¯min incubation at 70â¯Â°C. Copper content determination revealed a molar copper to protein ratio of 3.2 in the both sample. The present paper concerns the differences which are induced in enzyme structure after thermal treatment using common biochemical methods Intrinsic fluorescence of the enzyme was increased after incubation at 70â¯Â°C indicating higher compactness of the structure in comparison to untreated molecules. Quenching analysis did not show any significant changes in flexibility of the enzyme structure. The local changes in secondary structures were also obvious by far-UV circular dichroism when non-incubated and incubated laccase were compared. Oligomerization studies of the enzyme using gas-phase electrophoretic mobility macromolecule analysis (GEMMA) did not prove any oligomerization.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 109, 1 April 2018, Pages 49-56
Journal: International Journal of Biological Macromolecules - Volume 109, 1 April 2018, Pages 49-56
نویسندگان
Nasrin Mollania, Marjan Heidari, Khosro Khajeh,