BACKGROUND Recombinant protein purification is a crucial step for biochemistry and structural biology fields. Rapid robust purification methods utilize various peptide or protein tags fused to the target protein for affinity purification using corresponding matrices and to enhance solubility. However, affinity/solubility-tags often need to be removed in order to conduct functional and structura...

The intein-mediated purification system has the potential to significantly reduce the recovery costs of industrial recombinant proteins. The ability of inteins to catalyze a controllable peptide bond cleavage reaction can be used to separate a recombinant protein from its affinity tag during affinity purification. Inteins have been combined with a chitin-binding domain to serve as a self-cleavi...

BACKGROUND Recombinant protein expression and purification remains a fundamental issue for biotechnology. Recently we found that two short self-assembling amphipathic peptides 18A (EWLKAFYEKVLEKLKELF) and ELK16 (LELELKLKLELELKLK) can induce the formation of active protein aggregates in Escherichia coli (E. coli), in which the target proteins retain high enzymatic activities. Here we further exp...

BACKGROUND Many proteins form insoluble protein aggregates, called "inclusion bodies", when overexpressed in E. coli. This is the biggest obstacle in biotechnology. Ever since the reversible denaturation of proteins by chaotropic agents such as urea or guanidinium hydrochloride had been shown, these compounds were predominantly used to dissolve inclusion bodies. Other denaturants exist but have...

The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of ...

the goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native iranian microorganisms. at the end of screening program, a bacillus subtilis bp-36 strain producing thermophilic alkaline protease was isolated from a hot spring in ardebil province. the target enzyme was purified using a one-step aqueous two-phase systems (atps) prot...

the biodesulfurization (bds) of sulfur compounds in fossil fuels is a process to reduce sulfur dioxide emissions that cause environmental pollution. gordonia alkanivorans ripi90a is able to convert dibenzothiophene, an organic sulfur compound in petroleum, to 2-hydroxybiphenyl (2-hbp) in 4s pathway. in this study, (dbt), dsza and dszb, dbt sulfone monooxygenase, and desulfinase were respectivel...

after using 3 different generations of antibodies including human and non-human hyperimmune sera, monoclonal antibodies and chimeric antibodies, more recently a newer approach has been developed in which the antibody genes are cloned directly from a patient peripheral b-lymphocytes and expressed in a host like e. coli. in this study the candida albicans serotype a (nctc 3153) mannan was purifie...

an efficient method for purification of yard-glass shaped boron nitride nanotubes (yg-bnnts) fabricated via a chemical vapour reaction (cvr) route has been developed. impurities including carbon, boron nitride (bn), and fe species in the pristine yg-bnnt sample are removed by a combined physical and chemical procedure which involves ultrasonication, high temperature oxidation, hot-water washing...

background and objectives: proline dehydrogenase (prodh; 1.5.99.8) plays an important role in specific determination of plasma proline level in biosensor and diagnostic kits. the goal of this research was to isolate and characterize prodh enzyme from iranian soil microorganisms. materials and methods : screening of l-proline degradative enzymes from soil samples was carried out employing enrich...