Background: Many enzymes of industrial interest are not in the market since they are bioproduced as bacterial inclusion bodies, believed to be biologically inert aggregates of insoluble protein.
Protein aggregation is a major bottleneck during the bacterial production of recombinant proteins. In general, the induction of gene expression at sub-optimal growth temperatures improves the solubility of aggregation-prone polypeptides and minimizes inclusion body (IB) formation. However, the effect of low temperatures on the quality of the recombinant protein, especially within the insoluble cell fraction, has been hardly ever explored. In this work, we have examined the conformational status of a recombinant GFP protein when produced in Escherichia coli below 37 degrees C. As expected, the fraction of aggregated protein largely decreased at lower temperatures, while the conformational quality of both soluble and aggregated GFP, as reflected by its specific fluorescence emission, progressively improved. This observation indicates that physicochemical conditions governing protein folding affect concurrently the quality of the soluble and the aggregated forms of a misfolding-prone protein, and that protein misfolding and aggregation are clearly not coincident events.
The results of this study support the need to determine the optimum MB concentration and light parameters to maximize bacterial killing in root canals.
The main implication is that hospitals should implement a process-based organization to improve their efficiency. However, to actually achieve positive effects on efficiency, it is of paramount importance to observe some implementation rules, in particular to mobilize physician participation and to create an adequate organizational culture.
The antioxidant properties of two raw truffles (Terfezia claveryi Chatin and Picoa juniperi Vittadini) and five raw mushrooms (Lepista nuda, Lentinus edodes, Agrocybe cylindracea, Cantharellus lutescens, and Hydnum repandum) were tested by subjecting these truffles and mushrooms to different industrial processes (freezing and canning) and comparing them with common food antioxidants (alpha-tocopherol [E-307], BHA [E-320], BHT [E-321], and propyl gallate [E-310]) with regard to their ability to inhibit lipid oxidation. All of the truffles and mushrooms analyzed exhibited higher percentages of oxidation inhibition than did the food antioxidants according to assays based on lipid peroxidation (LOO*), deoxyribose (OH*), and peroxidase (H2O2). Frozen samples exhibited a small reduction in free radical scavenger activity, but the results did not show a significant difference (P < 0.05) with respect to the raw samples, while canned truffles and mushrooms lost some antioxidant activity as a consequence of industrial processing. All of the raw and frozen truffles and mushrooms except frozen Cantharellus improved the stability of oil against oxidation (100 degrees C Rancimat), while canned samples accelerated oil degradation. Antioxidant activity during 30 days of storage was measured by the linoleic acid assay, and all of the samples except canned Terfezia, Picoa, and Hydnum showed high or medium antioxidant activity. The Trolox equivalent antioxidant capacity assay was used to provide a ranking order of antioxidant activity as measured against that of Trolox (a standard solution used to evaluate equivalent antioxidant capacity). The order of raw samples with regard to antioxidant capacity was as follows (in decreasing order): Cantharellus, Agrocybe, Lentinus, Terfezia, Picoa, Lepista, and Hydnum. Losses of antioxidant activity were detected in the processed samples of these truffles and mushrooms.
Human cytomegalovirus (HCMV) infection promotes a persistent expansion of a function-Keywords: CD94/NKG2C r Cytomegalovirus r Human r NK cells r NKG2C genotype Additional supporting information may be found in the online version of this article at the publisher's web-site
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