The C-terminal domain of human alpha-fetoprotein (AFP‑3D) is a fragment that can be used as a vector for targeted delivery of drugs into tumor cells. A technique of recombinant human AFP‑3D refolding in the mobile phase of a gel‑filtration medium was developed and shown to produce a 90% yield of the target protein with confirmed functional activity.
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The anaerobic H2 production in the dark by bidirectional hydrogenase of unicellular cyanobacterium Synechocystis sp. strain PCC 6803 has been studied. D-glucose addition to cell suspension has been known to enhance H2 production, and the two mutants, glucose tolerant strain and its mutant lacking L-lactate dehydrogenase (LDH) gene, were introduced to improve H2 production with D-glucose. Higher D-glucose uptake rate of glucose tolerant strain resulted in higher H2 production rate comparing with
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Bacillus sp. SI-136, isolated from sodic-alkaline soil, showed 94% similarity to B. cereus group based on 16S rDNA sequence. It produced α-amylase of 26 kDa with maximum activity at pH 10.0, stable up to pH 12.0 and 80oC. Mn2+ enhanced its activity as also 10% NaCl in medium. Agricultural waste substrates supported growth and enzyme activity was enhanced by 30% with sugarcane bagasse. The partially purified enzyme showed efficient desizing of cotton fabric at 50oC (40-60 min) or 70oC (60 m
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