کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2021638 1069255 2008 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Affinity-based isolation of a bacterial lipase through steric chaperone interactions
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Affinity-based isolation of a bacterial lipase through steric chaperone interactions
چکیده انگلیسی

Lipases are important as additives in detergent formulations but their biocatalytic potential is increasingly exploited in the synthesis of high-added value chemicals, in fine-chemical production and in the pharmaceutical industry. Traditionally, conventional purification schemes comprise several chromatographic steps. Here we report a new purification procedure of the lipase (LipA) that is endogenously secreted by the Gram-negative bacterium Burkholderia glumae. This affinity purification combines the specific binding scaffold of a lipase-specific foldase (Lif) and the intrinsic resistance to chemical denaturation of LipA. The newly devised method is less labor-intensive, is fast, leads to a homogeneous preparation and can be easily scaled up. The novel and the conventional purification strategies were evaluated in parallel and characteristics of the B. glumae lipase were analyzed via CD spectroscopy. Lipopolysaccharide (LPS) was still present in the samples purified via the conventional purification scheme and was shown to increase the thermostability of the lipase.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 59, Issue 2, June 2008, Pages 342–348
نویسندگان
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