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Journal of Sciences Islamic Republic of Iran، جلد ۲۲، شماره ۲، صفحات ۱۰۵-۱۱۰
عنوان فارسی Synthesis and Production of Sweet-Tasting Protein in E. coli and Purification by Amylose Resin
چکیده فارسی مقاله A sweet water-soluble protein that reminds stable over wide ranges of temperature and pH, Brazzein has various applications. Its tastes like cane sugar but have no calories. However, the extraction of brazzein from its natural source is expensive and not applicable. In this study we used recombinant DNA technology to provide an alternative option for cheaper mass production of brazzein. A brazzein gene was designed, synthesized by using oligonucleotids and cloned into the pBlueScript vector. The synthetic fragment linked to the C-terminal of Maltose-binding protein (MBP) and Glutathion-S-Transferase (GST) for protein expression. The recombinant protein was expressed as a soluble form after induction by IPTG. The fusion protein was purified by amylose resin column and detected by SDS-PAGE. The best yields were achieved by producing brazzein as a fusion with MBP. MBP-brazzein system permits large-scale functional expression and purification of recombinant soluble proteins, providing a basis for the future study of structure and function of brazzein.
کلیدواژه‌های فارسی مقاله
عنوان انگلیسی Synthesis and Production of Sweet-Tasting Protein in E. coli and Purification by Amylose Resin
چکیده انگلیسی مقاله A sweet water-soluble protein that reminds stable over wide ranges of temperature and pH, Brazzein has various applications. Its tastes like cane sugar but have no calories. However, the extraction of brazzein from its natural source is expensive and not applicable. In this study we used recombinant DNA technology to provide an alternative option for cheaper mass production of brazzein. A brazzein gene was designed, synthesized by using oligonucleotids and cloned into the pBlueScript vector. The synthetic fragment linked to the C-terminal of Maltose-binding protein (MBP) and Glutathion-S-Transferase (GST) for protein expression. The recombinant protein was expressed as a soluble form after induction by IPTG. The fusion protein was purified by amylose resin column and detected by SDS-PAGE. The best yields were achieved by producing brazzein as a fusion with MBP. MBP-brazzein system permits large-scale functional expression and purification of recombinant soluble proteins, providing a basis for the future study of structure and function of brazzein.
کلیدواژه‌های انگلیسی مقاله Brazzein, recombinant protein, Sweet-tasting protein
نویسندگان مقاله f منصوری |
science and research branch, department of biology, islamic azad university
سازمان اصلی تایید شده: دانشگاه آزاد اسلامی علوم و تحقیقات (Islamic azad university science and research branch)

نشانی اینترنتی http://jsciences.ut.ac.ir/article_23032_37cfcc44a248c14daa93126a6f4cc197.pdf
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