کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
34821 45051 2014 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies
چکیده انگلیسی


• Magnetic-CLEAs (M-CLEAs) were prepared using PGA as enzyme model.
• M-CLEAs and CLEAs morphological structures and catalytic properties were compared.
• M-CLEAs magnetic recovery and reuse were perfect.

Biomolecules labeled with superparamagnetic nanoparticles can be selectively removed from complex reaction mixtures using an external magnetic field. Amino-functionalized superparamagnetic iron oxide nanoparticles (amino-SPION) were co-aggregated with penicillin G acylase and then cross-linked, generating magnetic cross-linked enzymes aggregates (M-CLEAs) that were quickly and efficiently recovered from the reaction medium by applying an external magnetic field. M-CLEAs and cross-linked enzymes aggregates (CLEAs) prepared under the same reaction conditions were characterized and compared. The best recovered activities were obtained for M-CLEAs prepared using polyethylene glycol 600 as precipitant and the most stable M-CLEA were obtained using tert-butanol. Successive penicillin G hydrolysis reactions were carried out using the same M-CLEA in a 50 mL reactor (3 reaction cycles), after the reactions the derivate was magnetically recovered without loss of activity demonstrating a total magnetic recovery. Line-scan energy dispersive X-ray spectroscopy showed that the amino-SPIONs were homogeneously dispersed within the structure of the M-CLEA.

Figure optionsDownload as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Process Biochemistry - Volume 49, Issue 1, January 2014, Pages 38–46
نویسندگان
, , , , , , , ,