Versatile Keratin Fibrous Adsorbents with Rapid-Response Shape-Memory Features for Sustainable Water Remediation.

Biodegradable shape-memory polymers derived from protein substrates are attractive alternatives with strong potential for valorization, although their reconstruction remains a challenge due to the poor processability and inherent instability. Herein, based on Maillard reaction and immobilization, a feather keratin fibrous adsorbent featuring dual-response shape-memory is fabricated by co-spinning with pullulan, heating, and air-assisted spraying ZIF-8-NH2. Maillard reaction between the amino group of keratin and the carbonyl group of pullulan improves the mechanics and thermal performance of the adsorbent. ZIF-8-NH2 immobilization endows the adsorbent with outstanding multipollutant removal efficiency (over 90%), water stability, and photocatalytic degradation and sterilization performance. Furthermore, the adsorbent can be folded to 1/12 of its original size to save space for transportation and allow for rapid on-demand unfolding (12 s) upon exposure to water and ultraviolet irradiation to facilitate the adsorption and photocatalytic activity with a larger water contact area. This research provides new insight for further applications of keratin-based materials with rapid shape-memory features.

Utilization of feather keratin waste to antioxidant and migration-enhancer peptides by Bacillus licheniformis 8-4.

AIMS: Feathers are keratin-rich byproducts of poultry processing, but those are often frequently abandoned as garbage and thus polluting the environment. Therefore, the study focused on the efficient biodegradation, bioactivity, and high-value application of feather keratin. METHODS AND RESULTS: Feather-degrading bacteria were identified, and the degradation properties were characterized. DPPH (1,1-Diphenyl-2-picrylhydrazyl radical) and ABTS (2,2'-Azino-bis (3-ethylbenzthiazoline-6-sulfonic acid))radical scavenging assays, cytotoxicity assays, intracellular reactive oxygen scavenging assays, and cell migration assays were used to examine the biological activities of the feather keratin hydrolysis peptides (FKHPs). The results showed that we screened a feather-degrading strain of Bacillus licheniformis 8-4, which achieved complete degradation of 2% (w/v) feathers within 48 h. Notably, the feather fermentation broth was particularly high in FKHPs, which exhibited good DPPH and ABTS radical scavenging ability. Further studies revealed that FKHPs had both the ability to scavenge H2O2-induced ROS from HaCat cells and the ability to promote HaCat cell migration, while remaining non-toxic. CONCLUSIONS: The effective feather-degrading ability of B. licheniformis 8-4 allowed for the fermentation of feather medium to yield active peptides that were both antioxidants and cell-migration enhancers.

Efficient adsorption of low-concentration uranium from aqueous solutions by biomass composite aerogel.

The development of nuclear energy has led to the depletion of uranium resources and now presents the challenge of treating radioactive wastewater. Extracting uranium from seawater and nuclear wastewater has been identified as an effective strategy for addressing these issues. However, extracting uranium from nuclear wastewater and seawater is still extremely challenging. In this study, an amidoxime-modified feather keratin aerogel (FK-AO aerogel) was prepared using feather keratin for efficient uranium adsorption. The FK-AO aerogel showed an impressive adsorption capacity of 585.88 mg·g-1 in an 8 ppm uranium solution, with a calculated maximum adsorption capacity of 990.10 mg·g-1. Notably, the FK-AO aerogel demonstrated excellent selectivity for U(VI) in simulated seawater that contained coexisting heavy metal ions. In a uranium solution having a salinity of 35 g·L-1 and a concentration of 0.1-2 ppm, the FK-AO aerogel achieved a uranium removal rate of greater than 90 %, indicating its effectiveness in adsorbing uranium in environments having high salinity and low concentration. This suggests that FK-AO aerogel is an ideal adsorbent for extracting uranium from seawater and nuclear wastewater, and it is also expected that it could be used in industrial applications for extracting uranium from seawater.

Agro-Industrial Protein Waste and Co-Products Valorization for the Development of Bioplastics: Thermoprocessing and Characterization of Feather Keratin/Gliadin Blends.

Biopolymers based on plant and animal proteins are interesting alternatives in the development of films with future prospects as food packaging. Considering that in recent years there has been an increasing interest in the valorization of agro-industrial residues and by-products and that the blending of polymers can lead to materials with improved properties, in this work, keratin-rich feather fibers and gliadins were blended at different ratios in order to develop sustainable and biodegradable films. Control gliadin G100, feather F100 films, and their blends at 3:1 (G75F25), 2:2 (G50F50), and 1:3 (G25F75) ratios were successfully developed through thermoprocessing. The physical properties were differentiated as a function of the concentration of both polymeric matrices. Although gliadins showed higher hydrophilicity as confirmed by their highest swelling degree, films with high gliadin ratios exhibited lower water vapor permeability values at low and medium relative humidities. On the other hand, the feather fiber-based films displayed the highest Young's modulus values and provided an oxygen barrier to the blends, principally at the highest relative humidity. In conclusion, the blend of these protein-based polymers at different ratio resulted in interesting composites whose physical properties could be adjusted.

Spectroscopy on the wing: Investigating possible differences in protein secondary structures in feather shafts of birds using Raman spectroscopy.

The central shaft of a bird's flight feather bears most of the aerodynamic load during flight and exhibits some remarkable mechanical properties. The shaft comprises two parts, the calamus and the rachis. The calamus is at the base of the shaft, while the rachis is the longer upper part which supports the vanes. The shaft is composed of a fibrous outer cortex, and an inner foam-like core. Recent nanoindentation experiments have indicated that reduced modulus values, Er, for the inner and outer regions of the cortex can vary, with the Er values of the inner region slightly greater than those of the outer region. In this work, Raman spectroscopy is used to investigate the protein secondary structures in the inner and outer regions of the feather cortex. Analysis of the Amide I region of Raman spectra taken from four birds (Swan, Gull, Mallard and Kestrel) shows that the ß-sheet structural component decreases between the inner and outer region, relative to the protein side-chain components. This finding is consistent with the proposal that Er values are greater in the inner region than the outer region. This work has shown that Raman spectroscopy can be used effectively to study the change in protein secondary structure between the inner and outer regions of a feather shaft.

Valorization of chicken feather waste into bioactive keratin hydrolysate by a newly purified keratinase from Bacillus sp. RCM-SSR-102.

The objective of this study is the characterization of a keratinase from Bacillus sp.RCM-SSR-102 and its application in the preparation of keratin hydrolysate from chicken feather waste. The purified KER102 keratinase was characterized as a serine-metallo protease having a molecular weight of 30 kDa with optimum pH and temperature of 10 and 50 °C respectively. The keratinase could retain 98% activity at pH 10 and above and 55% activity at 20% salt concentration. The KER102 keratinase was found to be stable in the presence of oxidizing agents, surfactants and organic solvents. The keratinase could also hydrolyze both soluble and insoluble complex protein substrates. The KER102 keratinase could hydrolyze up to 5% (w/v) feather releasing 1.7 ± 0.19 mg/mL soluble peptides. The feather keratin hydrolysate (FKH) had both antioxidant and antityrosinase activity. The IC50 value of FKH in 2, 2-diphenyl 1-picrylhydrazyl (DPPH) radical scavenging activity (1.02 ± 0.01 mg/mL), 2'-azino-bis-3-ethylbenzothiazoline-6-sulphonic acid (ABTS) radical scavenging activity (20 ± +00.04 µg/mL) and anti-tyrosinase activity (1.2 ± 0.22 mg/mL) was recorded. The FKH also had DNA protecting ability against oxidative damage. Antioxidant and anti-tyrosinase compounds have potential applications in the pharmaceutical and cosmeceutical industry. Hence, the purified keratinase can be a potential candidate for the production of antioxidant and antityrosinase compounds from chicken feather waste.

Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production.

Feathers account for 5-7% of the total weight of chicken have become one of the major pollutants due to their recalcitrant nature. Feather which is constituted of 90% keratin can be a good source of peptides, amino acids, and minerals for use as organic fertilizer. Traditional feather degradation methods consume large amount of energy and reduces the overall quality of the proteins. However, degradation of keratin by keratinolytic bacteria may represent as an alternative for the development of cheap, cost effective, eco-friendly, and easily available nitrogen (N) and minerals rich source as potential organic fertilizers. Keratinase enzymes from bacteria are serine-type proteases showing optimal activity at pH 6 to 9 and 30 to 50 °C. Mechanism of degradation includes, sulfitolysis, proteolysis, followed by deamination. Keratinolytic bacteria showing antagonism against important plant pathogens may act as biocontrol agent. Feather hydrolyzate can also be employed as nitrogenous fertilizers for plant growth. Tryptophan release from the feather degradation can act as precursor for plant phytohormone, indole-3-acetic acid (IAA). Solubilization of inorganic phosphate (P) by keratinolytic bacteria may further elevate the growth of plant. Application of hydrolyzate increases the water holding capacity, N, carbon (C) and mineral content of the soil. It elevates protein, amino acids, and chlorophyll content of plant. Feather hydrolyzate enhances seed germination and growth of plant. Soil application further increases the population of beneficial bacteria. The use of keratinolytic bacteria having antagonistic and plant growth promoting activities, and feather hydrolyzate can emerge as sustainable and alternative tools to promote and improve organic farming, agro-ecosystem, environment, human health, and soil biological activities.

Transcriptional profiling of liver in riboflavin-deficient chicken embryos explains impaired lipid utilization, energy depletion, massive hemorrhaging, and delayed feathering.

BACKGROUND: A strain of Leghorn chickens (rd/rd), unable to produce a functional riboflavin-binding protein, lays riboflavin-deficient eggs, in which all embryos suddenly die at mid-incubation (days 13-15). This malady, caused by riboflavin deficiency, leads to excessive lipid accumulation in liver, impaired ß-oxidation of lipid, and severe hypoglycemia prior to death. We have used high-density chicken microarrays for time-course transcriptional scans of liver in chicken embryos between days 9-15 during this riboflavin-deficiency-induced metabolic catastrophe. For comparison, half of rd/rd embryos (n = 16) were rescued from this calamity by injection of riboflavin just prior to incubation of fertile eggs from rd/rd hens. RESULTS: No significant differences were found between hepatic transcriptomes of riboflavin-deficient and riboflavin-rescued embryos at the first two ages (days 9 and 11). Overall, we found a 3.2-fold increase in the number of differentially expressed hepatic genes between day 13 (231 genes) and day 15 (734 genes). Higher expression of genes encoding the chicken flavoproteome was more evident in rescued- (15 genes) than in deficient-embryos (4 genes) at day 15. Diminished activity of flavin-dependent enzymes in riboflavin-deficient embryos blocks catabolism of yolk lipids, which normally serves as the predominant source of energy required for embryonic development. CONCLUSIONS: Riboflavin deficiency in mid-stage embryos leads to reduced expression of numerous genes controlling critical functions, including ß-oxidation of lipids, blood coagulation and feathering. Surprisingly, reduced expression of feather keratin 1 was found in liver of riboflavin-deficient embryos at e15, which could be related to their delayed feathering and sparse clubbed down. A large number of genes are expressed at higher levels in liver of riboflavin-deficient embryos; these up-regulated genes control lipid storage/transport, gluconeogenesis, ketogenesis, protein catabolism/ubiquitination and cell death.

Filamentous Structure of Hard ß-Keratins in the Epidermal Appendages of Birds and Reptiles.

The structures of avian and reptilian epidermal appendages, such as feathers, claws and scales, have been modelled using X-ray diffraction and electron microscopy data, combined with sequence analyses. In most cases, a family of closely related molecules makes up the bulk of the appendage, and each of these molecules contains a central ß-rich 34-residue segment, which has been identified as the principal component of the framework of the 3.4 nm diameter filaments. The N- and C-terminal segments form the matrix component of the filament/matrix complex. The 34-residue ß-rich central domains occur in pairs, related by either a parallel dyad or a perpendicular dyad axis, and form a ß-sandwich stabilized by apolar interactions. They are also twisted in a right-handed manner. In feather, the filaments are packed into small sheets and it is possible to determine their likely orientation within the sheets from the low-angle X-ray diffraction data. The physical properties of the various epidermal appendages can be related to the amino acid sequence and composition of defined molecular segments characteristic of the chains concerned.

Fifty years of fibrous protein research: a personal retrospective.

As a result of X-ray fiber diffraction studies on fibrous proteins and crystallographic data on fragments derived from them, new experimental techniques across the biophysical and biochemical spectra, sophisticated computer modeling and refinement procedures, widespread use of bioinformatics and improved specimen preparative procedures the structures of many fibrous proteins have now been determined to at least low resolution. In so doing these structures have yielded insight into the relationship that exists between sequence and conformation and this, in turn, has led to improved methodologies for predicting structure from sequence data alone. In this personal retrospective a selection of progress made during the past 50years is discussed in terms of events to which the author has made some contribution.

Morphological, Thermal, and Mechanical Properties of Nanocomposites Based on Bio-Polyamide and Feather Keratin-Halloysite Nanohybrid.

One solution to comply with the strict regulations of the European Commission and reduce the environmental footprint of composites is the use of composite materials based on bio-polymers and fillers from natural resources. The aim of our work was to obtain and analyze the properties of bio-polymer nanocomposites based on bio-PA (PA) and feather keratin-halloysite nanohybrid. Keratin (KC) was mixed with halloysite (H) as such or with the treated surface under dynamic conditions, resulting in two nanohybrids: KCHM and KCHE. The homogenization of PA with the two nanohybrids was conducted using the extrusion processing process. Two types of nanocomposites, PA-KCHM and PA-KCHE, with 5 wt.% KC and 1 wt.% H were obtained. The properties were analyzed using SEM, XRD, FTIR, RAMAN, TGA, DSC, tensile/impact tests, DMA, and nanomechanical tests. The best results were obtained for PA-KCHE due to the stronger interaction between the components and the uniform dispersion of the nanohybrid in the PA matrix. Improvements in the modulus of elasticity and of the surface hardness by approx. 75% and 30%, respectively, and the resistance to scratch were obtained. These results are promising and constitute a possible alternative to synthetic polymer composites for the automotive industry.

Exploring keratin composition variability for sustainable thermal insulator design.

In pursuing sustainable thermal insulation solutions, this study explores the integration of human hair and feather keratin with alginate. The aim is to assess its potential in thermal insulation materials, focusing on the resultant composites' thermal and mechanical characteristics. The investigation uncovers that the type and proportion of keratin significantly influence the composites' porosity and thermal conductivity. Specifically, higher feather keratin content is associated with lesser sulfur and reduced crosslinking due to shorter amino acids, leading to increased porosity and pore sizes. This, in turn, results in a decrease in ß-structured hydrogen bond networks, raising non-ordered protein structures and diminishing thermal conductivity from 0.044 W/(m·K) for pure alginate matrices to between 0.033 and 0.038 W/(m·K) for keratin-alginate composites, contingent upon the specific ratio of feather to hair keratin used. Mechanical evaluations further indicate that composites with a higher ratio of hair keratin exhibit an enhanced compressive modulus, ranging from 60 to 77 kPa, demonstrating the potential for tailored mechanical properties to suit various applications. The research underscores the critical role of sulfur content and the crosslinking index within keratin's structures, significantly impacting the thermal and mechanical properties of the matrices. The findings position keratin-based composites as environmentally friendly alternatives to traditional insulation materials.

Effective biodegradation on chicken feather by the recombinant KerJY-23 Bacillus subtilis WB600: A synergistic process coupled by disulfide reductase and keratinase.

Keratin wastes are abundantly available but rich in hard-degrading fibrous proteins, and the keratinase-producing microorganisms have gained significant attention due to their biodegradation ability against keratinous materials. In order to improve the degradation efficiency of feather keratins, the keratinase gene (kerJY-23) from our previously isolated feather-degrading Ectobacillus sp. JY-23 was overexpressed in Bacillus subtilis WB600 strain. The recombinant KerJY-23 strain degraded chicken feathers rapidly within 48 h, during which the activities of disulfide reductase and keratinase KerJY-23 were sharply increased, and the free amino acids especially the essential phenylalanine and tyrosine were significantly accumulated in feather hydrolysate. The results of structural characterizations including scanning electron microscopy, Fourier transform infrared spectrum, X-ray diffraction, and X-ray photoelectron spectroscopy, demonstrated that the feather microstructure together with the polypeptide bonds and SS bonds in feather keratins were attacked and destroyed by the recombinant KerJY-23 strain. Therefore, the recombinant KerJY-23 strain contributed to feather degradation through the synergistic action of the secreted disulfide reductase to break the SS bonds and keratinase (KerJY-23) to hydrolyze the polypeptide bonds in keratins. This study offers a new insight into the underlying mechanism of keratin degradation, and provides a potential recombinant strain for the valorization of keratin wastes.

Novel Antioxidant Peptides Derived from Feather Keratin Alleviate H2O2-Induced Oxidative Damage in HepG2 Cells via Keap1/Nrf2 Pathway.

Reactive oxygen species (ROS) are crucial for signal transduction and the maintenance of cellular homeostasis. However, superfluous ROS may engender chronic pathologies. Feather keratin is a promising new source of antioxidant peptides that can eliminate excess ROS and potentially treat oxidative stress-related diseases, but the underlying mechanisms have remained elusive. This study investigated the antioxidant effects and mechanisms against H2O2-induced oxidative damage in HepG2 cells of the two latest discovered antioxidant peptides, CRPCGPTP (CP-8) and ANSCNEPCVR (AR-10), first decrypted from feather keratin. The results revealed that CP-8 and AR-10 did not exhibit cytotoxicity to HepG2 cells while reducing intracellular ROS accumulation. Simultaneously, they enhanced the activities of catalase (CAT), superoxide dismutase (SOD), and glutathione peroxidase (GSH-Px), thus alleviating H2O2-induced cell apoptosis. Molecular docking analysis demonstrated that CP-8, AR-10 interacted well with the key amino acids in the Kelch domain of Keap1, thereby directly disrupting the Keap1-Nrf2 interaction. The peptides' biosafety and antioxidant activity via Keap1/Nrf2 signaling lay the groundwork for further animal studies and applications as functional food additives.

Edible pullulan enhanced water-soluble keratin with improved sizing performance for sustainable textile industry.

Feather keratin from waste feather has become an attractive target to replace petroleum-based Poly (vinyl alcohol) sizes due to its easy film-forming ability, excellent adhesive property, biodegradability and low cost. However, poor water-solubility and brittleness of pure keratin films have become the bottlenecks and restricted the application of keratin as sizing agents. Therefore, water-soluble keratin was extracted by the reduction-preservation method and enhanced by saccharides in aqueous system to obtain all-green keratin-based slurry. The results showed that the keratin-based slurry exhibited improved sizing performance in the order of sucrose ≤ glucose ≤ pullulan by the moderate Maillard reaction. Among them, the fabricated pullulan-keratin sizes films had 27.86 %, 2684.08 % and 2911.31 % increment in tensile strength, elongation and work of facture compared with pure keratin sizes films. Besides, the addition of pullulan and subsequently moderate Maillard reaction improved the thermo-tenacity of keratin-based sizes, which was expected to tackle with the brittleness of pure keratin size films. In addition, novel pullulan-keratin sizes had good sizing performance and high desizing efficiency to cotton, cotton/polyester and polyester yarns and fabrics. Successful utilization of pullulan-keratin sizes will bring opportunities for high value utilization of waste feather and promote the green and low-carbon development of textile industry.

Preparation, Purification, and Identification of Novel Feather Keratin-Derived Peptides with Antioxidative and Xanthine Oxidase Inhibitory Activities.

Feather keratin is an underappreciated protein resource of high quality, with limited bioavailability, and it urgently requires eco-friendly methods to enhance its value. Here, we report on the preparation, purification, and identification of novel peptides with antioxidant and xanthine oxidase (XOD) inhibitory activities from fermented feather broth, using Bacillus licheniformis 8-4. Two peptides, namely, DLCRPCGPTPLA (DA-12) and ANSCNEPCVR (AR-10), displayed remarkable 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) radical scavenging abilities with half-maximal inhibitory concentrations (IC50) values of 0.048, 0.034, and 0.95, 0.84 mg/mL, respectively. These values exceed those of the previously reported feather keratin-derived antioxidant peptides. Another peptide, GNQQVHLQSQDM (GM-12), demonstrated XOD activity inhibition, with an IC50 value of 12.15 mg/mL, and it quenched the fluorescence of XOD. Furthermore, after simulating gastrointestinal digestion, DA-12, AR-10, and GM-12 retained their biological activities. Meanwhile, DA-12 and GM-12 showed an unexpected synergistic inhibition on XOD activity accompanied by fluorescence quenching. This study provides new insights into the potential applications of feather keratin, including functionalized feed with antioxidative and antigout (anti-hyperuricemia) activities.

Prospective study relating genotype profiles with race performance in racing pigeons.

This is a prospective study to investigate the impact of genotype profiles on race performance in racing pigeons. Genotypes studied included lactate dehydrogenase A (LDHA), dopamine receptor (DRD), myostatin (MSTN), and feather keratin (F-KER), as well as demographic factors such as gender, color, and the mtDNA. This study shows differences within genotypes DRD456 (P = 0.027) and F-KER (P = 0.018). For DRD456, race coefficients were lower (= better performance) for genotype CT. For F-KER, race coefficients were lower for GG, overall, while within the F-KER TT genotype race performance was best at longer distances. After including Queen L mtDNA in the model, both the effects of F-KER and DRD456 remained significant. The effect of Queen L mtDNA alone was significant (P = 0.004) and mainly driven by the effect in short distance races. In addition, birds with the checker color check had a lower race coefficient than birds with the color blue bar (P = 0.0012). Also, this effect was independently significant and remained significant in the multivariate analysis. No differences in race coefficients were seen between genotypes for LDHA and MSTN nor for the demographic factor of gender. While individual factors were related to differences in race performance, and although one could be tempted to favor a bird with DRD4 CCCT-F-KER TT-LDHA AB-checker color for long distance races, further and larger prospective studies including birds unrelated to our family of birds will be needed to confirm our findings and to determine a superior profile including multiple genetic factors.

Newer guar gum ester/chicken feather keratin interact films for tissue engineering.

This work intends to synthesis newer guar gum indole acetate ester and design film scaffolds based on protein-polysaccharide interactions for tissue engineering applications. Guar gum indole acetate(GGIA) was synthesized for the first time from guar gum in presence of aprotic solvent activated hofmeister ions. The newer biopolymer was fully characterized in FT-IR,13C NMR, XRD and TGA analysis. High DS (Degree of Substitution, DS = 0.61) GGIA was cross-linked with hydrolyzed keratin, extracted from chicken feather wastes. Films were synthesized from different biopolymer ratios and the surface chemistry appeared interesting. Physicochemical properties for GGIA-keratin association were notable. Fully bio-based films were non-cytotoxic and exhibited excellent biocompatibility for human dermal fibroblast cell cultivations. The film scaffold showed 63% porosity and the recorded tensile strength at break was 6.4 MPa. Furthermore, the standardised film exerted superior antimicrobial activity against both the Gram-positive and Gram-negative bacteria. MICs were recorded at 130 µg/mL and 212 µg/mL for E. coli and S. aureus respectively. In summary, GGIA-keratin film scaffolds represented promising platforms for skin tissue engineering applications.

Preparation and Characterization of Edible Dialdehyde Carboxymethyl Cellulose Crosslinked Feather Keratin Films for Food Packaging.

The development of edible films based on the natural biopolymer feather keratin (FK) from poultry feathers is of great interest to food packaging. Edible dialdehyde carboxymethyl cellulose (DCMC) crosslinked FK films plasticized with glycerol were prepared by a casting method. The effect of DCMC crosslinking on the microstructure, light transmission, aggregate structure, tensile properties, water resistance and water vapor barrier were investigated. The results indicated the formation of both covalent and hydrogen bonding between FK and DCMC to form amorphous FK/DCMC films with good UV-barrier properties and transmittance. However, with increasing DCMC content, a decrease in tensile strength of the FK films indicated that plasticization, induced by hydrophilic properties of the DCMC, partly offset the crosslinking effect. Reduction in the moisture content, solubility and water vapor permeability indicated that DCMC crosslinking slightly reduced the moisture sensitivity of the FK films. Thus, DCMC crosslinking increased the potential viability of the FK films for food packaging applications, offering a value-added product.

A sodium alginate/feather keratin composite fiber with skin-core structure as the carrier for sustained drug release.

To alleviate the serious gastrointestinal side reaction of indomethacin (IDM), sodium alginate/feather keratin (SA/FK) fiber with skin-core structure was prepared via wet spinning as the carrier for sustained release of IDM. Fourier translation infrared (FT-IR) spectroscopy was adopted to investigate the reaction mechanism among SA, FK and IDM, and Ultraviolet-visible (UV-Vis) spectroscopy was used to systematically evaluate the sustained release capacity of SA/FK fiber in three simulated fluids. Scanning electron microscope (SEM) was employed to observe the apparent morphology of SA/FK fiber. The results indicate that, release amount of IDM exhibits an increase trend along with time; the release amount of IDM reaches 80% after 12 h in colon fluid and small intestinal fluid, and is less than 20% in digestive fluid. Simultaneously, FK can effectively control the release of IDM, and with the increase of FK content, IDM release time of the carrier fiber extends.