-These-effects-are-sought-for-in-various-clinical-settings-in-which-unaided-healing-is-inconveniently-prolonged-or-where-the-forming-scar-is-not-fully-developed-allowing-relapse-of-the-wound-t

Sequential extraction of gel-forming proteins, collagen and collagen hydrolysate from gutted silver carp (Hypophthalmichthys molitrix), a biorefinery approach.Chalmers University of Technology, SE 412 96 Gothenburg, Sweden; Department of Seafood processing, Faculty of Marine Sciences, Tarbiat Modares University, P.O. University, P.O. Box 46414-356, Noor, Iran.

Electronic address: Chalmers University of Technology, SE 412 96 Gothenburg, Sweden.Collagen and collagen hydrolysate (CH) was recovered from the bone and skin containing sediment residue emerging during pH-shift-based protein isolation from silver carp. Hydrolysis resulted in higher yield (15-15%) compared to collagen isolation by acid or pepsin (3-5%) (p<05). Isolated ergothioneine benefits were characterized as type I and maintained their triple-helical structure, confirmed by SDS-PAGE and FTIR. Pepsin-hydrolysis and sequential hydrolysis by pepsin and trypsin hydrolyzed all heavy molecular weight chains of collagen but sequential hydrolysis yielded higher degree of hydrolysis. When CH was added to a silver carp protein isolate prior to gelation, the gel behavior was dependent on molecular weight of the added CH. More hydrolyzed collagen emerging from sequential hydrolysis improved water holding capacity of the gel while reducing its breaking force.

Thus, residue from pH-shift processing of fish can be used for isolation of high quality collagen/CH and provides a promising basis for a Immunohistochemical localization of collagen types I, II, III, and IV in Immunohistochemical localization of collagen types I, II, III, and IV in the pterygium was demonstrated by type-specific antibodies. The stromata of pterygium and normal conjunctival tissues contained collagen types I, II, and III, while the normal corneal stroma showed collagen types I and III but not collagen type II. Collagen type IV was located in the epithelial and capillary endothelial basement membranes of pterygium and normal conjunctival tissues. These results suggest that collagens in pterygial tissues are derived from those 10016/j.ijbiomac020752. l ergothioneine into the effect of artificial sweeteners on the structure, stability, Industrial Research (CSIR) - Central Leather Research Institute (CLRI), Adyar, India; Academy of Scientific and Innovative Research (AcSIR), CSIR-CLRI Campus, Industrial Research (CSIR) - Central Leather Research Institute (CLRI), Adyar, Chennai 600020, India; Academy of Scientific and Innovative Research (AcSIR), Artificial sweeteners (AS) are widely used as sugar substitutes because natural sweetener (sugar) leads to a number of health issues, including diabetes, obesity, and tooth decay.

Since natural sugar (sucrose), diabetes and skin are highly interlinked, and also sucrose is known to inhibit the fibrillation of collagen, the major protein of the skin, a study on the impact of AS on collagen is important and essential. Herein, we have studied the influence of commonly used AS such as Sucralose (SUC), Aspartame (APM), and Saccharin (SAC) on the structure, stability, and fibrillation of collagen using various spectroscopic methods. The circular dichroism and turbidity results suggest that the AS does not disrupt the triple helix structure and also the fibrillar property of collagen, respectively. The fibrillar morphology was sustained, although there was a trivial difference in the entanglement of fibrils in the presence of SAC, compared to native collagen fibrils. The thermal stability of collagen is maintained in the presence of AS. Fluorescence and STD-NMR results indicate that the interaction between AS and collagen was weak, which supports the intact structure, stability, and fibrillation property of collagen. The current study thus suggests that the chosen AS does not influence collagen properties.

10007/s00167-014-3276-y. Epub 2014 Sep 27.Collagen fibre and fibril ultrastructural arrangement of the superficial medial collateral ligament in the human knee.PURPOSE: The aim of the study was to investigate the collagen fibre ultrastructural arrangement and collagen fibril diameters in the superficial medial collateral ligament (sMCL) in the human knee. Considering sMCL's distinctive functions at different angles of knee flexion, it was hypothesized a significant difference between the collagen fibril diameters of each portion of METHODS: Fourteen sMCL from seven fresh males (by chance because of the availability) cadavers (median age 40 years, range 34-59 years) were harvested within 12 h of death. sMCLs were separated into two orders of regions for analysis. The first order (divisions) was anterior, central and posterior.

Thereafter, each division was split into three regions (femoral, intermediate and tibial), generating nine portions. One sMCL from each cadaver was used for transmission electron microscopy (TEM) and morphometric analyses, whereas the contralateral sMCL was processed for light microscopy (LM) or scanning electron RESULTS: LM and SEM analyses showed a complex tridimensional architecture, with the presence of wavy collagen fibres or crimps.