Keratin - Based materials for biomedical applications

Feroz, Sandleen; Muhammad, Nawshad; Ratnayake, Jithendra; Dias, George J.

doi:10.1016/j.bioactmat.2020.04.007

Cited by 247 publications

(177 citation statements)

References 165 publications

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“…Keratins also possess the tripartite structure uniformly shared among the IF proteins: "a highly conserved central α-helical rod domain flanked by a nonα-helical amino-terminal head domain and carboxy-terminal tail domain" (Nafeey et al, 2016). The unique pliable nature of IFs forms the basis for their role as a mechanical cushion that shields cells from external stressors (Leitner et al, 2012;Feroz et al, 2020). Additionally, keratin may be formed by the aggregation of coiled heterodimers consisting of an acidic and a basic subunit that are organized in an antiparallel manner.…”

Section: Structural Complexity Of Keratinmentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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The search for novel renewable products over synthetics hallmarked this decade and those of the recent past. Most economies that are prospecting on biodiversity for improved bio-economy favor renewable resources over synthetics for the potential opportunity they hold. However, this field is still nascent as the bulk of the available resources are non-renewable based. Microbial metabolites, emphasis on secondary metabolites, are viable alternatives; nonetheless, vast microbial resources remain under-exploited; thus, the need for a continuum in the search for new products or bio-modifying existing products for novel functions through an efficient approach. Environmental distress syndrome has been identified as a factor that influences the emergence of genetic diversity in prokaryotes. Still, the process of how the change comes about is poorly understood. The emergence of new traits may present a high prospect for the industrially viable organism. Microbial enzymes have prominence in the bio-economic space, and proteases account for about sixty percent of all enzyme market. Microbial keratinases are versatile proteases which are continuously gaining momentum in biotechnology owing to their effective bio-conversion of recalcitrant keratin-rich wastes and sustainable implementation of cleaner production. Keratinase-assisted biodegradation of keratinous materials has revitalized the prospects for the utilization of cost-effective agro-industrial wastes, as readily available substrates, for the production of high-value products including amino acids and bioactive peptides. This review presented an overview of keratin structural complexity, the potential mechanism of keratin biodegradation, and the environmental impact of keratinous wastes. Equally, it discussed microbial keratinase; vis-à-vis sources, production, and functional properties with considerable emphasis on the ecological implication of microbial producers and catalytic tendency improvement strategies. Keratinase applications and prospective high-end use, including animal hide processing, detergent formulation, cosmetics, livestock feed, and organic fertilizer production, were also articulated.

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Section: Structural Complexity Of Keratinmentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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“…The type of polymer influences the microbial community composition of the associated biofilm. For example, keratin-based biopolymers are being extensively explored for biomedical applications [26][27][28]. However, they may also be more susceptible to bacterial colonization, since Proteobacteria have been shown to colonize keratin-rich surfaces such as the shells of freshwater turtles [29].…”

Section: Introductionmentioning

confidence: 99%

Expression of a Shiga-Like Toxin during Plastic Colonization by Two Multidrug-Resistant Bacteria, Aeromonas hydrophila RIT668 and Citrobacter freundii RIT669, Isolated from Endangered Turtles (Clemmys guttata)

et al. 2020

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Aeromonas hydrophila RIT668 and Citrobacter freundii RIT669 were isolated from endangered spotted turtles (Clemmys guttata). Whole-genome sequencing, annotation and phylogenetic analyses of the genomes revealed that the closest relative of RIT668 is A. hydrophila ATCC 7966 and Citrobacter portucalensis A60 for RIT669. Resistome analysis showed that A. hydrophila and C. freundii harbor six and 19 different antibiotic resistance genes, respectively. Both bacteria colonize polyethylene and polypropylene, which are common plastics, found in the environment and are used to fabricate medical devices. The expression of six biofilm-related genes—biofilm peroxide resistance protein (bsmA), biofilm formation regulatory protein subunit R (bssR), biofilm formation regulatory protein subunit S (bssS), biofilm formation regulator (hmsP), toxin-antitoxin biofilm protein (tabA) and transcriptional activator of curli operon (csgD)—and two virulence factors—Vi antigen-related gene (viaB) and Shiga-like toxin (slt-II)—was investigated by RT-PCR. A. hydrophila displayed a >2-fold increase in slt-II expression in cells adhering to both polymers, C. freundii adhering on polyethylene displayed a >2-fold, and on polypropylene a >6-fold upregulation of slt-II. Thus, the two new isolates are potential pathogens owing to their drug resistance, surface colonization and upregulation of a slt-II-type diarrheal toxin on polymer surfaces.

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“…Keratin can be extracted from natural materials by different processes such as the use of ionic liquids [ 52 ], microwave irradiation [ 53 ], alkaline treatment [ 54 ], and reduction of disulphide linkage [ 55 ]. Capability of keratin to self-assemble and support cellular proliferation enhance its use in tissue regeneration applications [ 50 , 56 ]. Between them, the reconstruction or regeneration of ocular surface [ 57 ], urinary track [ 58 ], and nerves [ 59 ] are significant.…”

Section: Biomimetic Hybrid Systems Based On Natural Polymers For Tmentioning

confidence: 99%

Biomimetic Hybrid Systems for Tissue Engineering

2020

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Tissue engineering approaches appear nowadays highly promising for the regeneration of injured/diseased tissues. Biomimetic scaffolds are continuously been developed to act as structural support for cell growth and proliferation as well as for the delivery of cells able to be differentiated, and also of bioactive molecules like growth factors and even signaling cues. The current research concerns materials employed to develop biological scaffolds with improved features as well as complex preparation techniques. In this work, hybrid systems based on natural polymers are discussed and the efforts focused to provide new polymers able to mimic proteins and DNA are extensively explained. Progress on the scaffold fabrication technique is mentioned, those processes based on solution and melt electrospinning or even on their combination being mainly discussed. Selection of the appropriate hybrid technology becomes vital to get optimal architecture to reasonably accomplish the final applications. Representative examples of the recent possibilities on tissue regeneration are finally given.

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Keratin - Based materials for biomedical applications

Cited by 247 publications

References 165 publications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Expression of a Shiga-Like Toxin during Plastic Colonization by Two Multidrug-Resistant Bacteria, Aeromonas hydrophila RIT668 and Citrobacter freundii RIT669, Isolated from Endangered Turtles (Clemmys guttata)

Biomimetic Hybrid Systems for Tissue Engineering

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