Composite biomaterials based on proteins and inorganic fillers are highly attractive for wound dressing applications due to their highly absorbent properties towards blood and exudate provided by the inorganic fillers. Moreover, such composites offer a desirable environment for cells due to the combination of organic and inorganic characteristics. This study highlights the fabrication of soy protein isolate/nanoscale bioactive glass composite films by solvent casting method as a matrix for wound-dressing applications. The effect of the addition of bioactive glass nano particles on blood clotting was assessed. Cytotoxicity and in vitro cytocompatibility of the films were also tested. The results showed that the composite films could meet the essential requirements for an appropriate wound dressing with additional favorable properties such as hemostatic capability and mechanical properties as well as significant cell cytocompatibility.
Jack bean (Canavalia ensiformis) seeds contain several biologically important proteins among which α-mannosidase (EC 3.2.1.24) has been purified, its biochemical properties studied and widely used in glycan analysis. In the present study, we have used the purified enzyme and derived its amino acid sequence covering both the known subunits (molecular mass of ∼66,000 and ∼44,000 Da) hitherto not known in its entirety. Peptide de novo sequencing and structural elucidation of N-glycopeptides obtained either directly from proteolytic digestion or after zwitterionic hydrophilic interaction liquid chromatography solid phase extraction-based separation were performed by use of nanoelectrospray ionization quadrupole time-of-flight mass spectrometry and low-energy collision-induced dissociation experiments. De novo sequencing provided new insights into the disulfide linkage organization, intersection of subunits and complete N-glycan structures along with site specificities. The primary sequence suggests that the enzyme belongs to glycosyl hydrolase family 38 and the N-glycan sequence analysis revealed high-mannose oligosaccharides, which were found to be heterogeneous with varying number of hexoses viz, Man8-9GlcNAc2 and Glc1Man9GlcNAc2 in an evolutionarily conserved N-glycosylation site. This site with two proximal cysteines is present in all the acidic α-mannosidases reported so far in eukaryotes. Further, a truncated paucimannose type was identified to be lacking terminal two mannose, Man1(Xyl)GlcNAc2 (Fuc).
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