Utilization of feather keratin waste to antioxidant and migration-enhancer peptides byBacillus licheniformis8-4

Abstract

Aims Feathers are keratin-rich byproducts of poultry processing but that are often frequently abandoned as garbage and 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 and ABTS 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 B. 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 to promote HaCat cell migration, while remaining non-toxicity. 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 antioxidant and pro-cell migration.

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

“…Feathers, which are the primary byproduct of poultry processing, contain a high proportion of proteins (≥90%), including essential amino acids, making them a valuable source of nutrition. , However, feather keratin, which is a particularly resistant protein, is often disposed of in an unregulated manner, leading to environmental pollution and limiting its potential applications. , Therefore, there is an urgent need to develop environmentally friendly and cost-effective strategies to exploit the high value-added products of feather keratin. Recent studies have shown that hydrolysate peptides derived from feather keratin (FKHPs) possess significant antioxidant activity, as demonstrated by their excellent DPPH and ABTS radical scavenging capacities, as well as their ability to scavenge intracellular ROS. − These peptides are also rich in hydrophobic amino acids, which are a characteristic component of uric acid-lowering peptides that have been previously identified, including XOD inhibitory peptides. ,, Thus, we hypothesize that FKHPs may be an ideal source of uric acid-lowering peptides, yet to date, no XOD inhibitory peptides have been identified from FKHPs.…”

“…Regrettably, these methods often result in energy consumption, environmental pollution, and high costs . In our laboratory, a proficient feather-degrading strain of Bacillus licheniformis 8-4 was screened, which can fully degrade feathers within 48 h, yielding up to 2.62 g FKHPs per 10 g of feathers, with a conversion rate of 26.2% . Hence, it is a promising alternative to produce FKHPs via fermentation of B.…”

“…26 In our laboratory, a proficient feather-degrading strain of Bacillus licheniformis 8-4 was screened, which can fully degrade feathers within 48 h, yielding up to 2.62 g FKHPs per 10 g of feathers, with a conversion rate of 26.2%. 23 Hence, it is a promising alternative to produce FKHPs via fermentation of B. licheniformis 8-4 utilizing feather as the exclusive source of carbon, nitrogen, and energy.…”

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

“…Our previous studies have demonstrated that feather keratin fermentation using Bacillus licheniformis 8− 4 yields feather keratin hydrolytic peptides with strong antioxidant activities in vitro. 17 Using ultrafiltration, HPLC purification, and LC/MS-MS identification, two novel peptides, CRPCGPTP (CP-8) and ANSCNEPCVR (AR-10), were isolated and exhibited significant antioxidant activity. Specifically, CP-8 exhibited IC 50 values of 0.92 and 0.033 mg/ mL for scavenging ABTS and DPPH radicals, respectively, while AR-10 showed IC 50 values of 0.84 and 0.034 mg/mL for eliminating ABTS and DPPH radicals, respectively.…”

“…In recent years, an increasing number of research teams have prepared bioactive peptides with antioxidant, antiaging, and antihypertensive properties from feather keratins through fermentation or composite enzymatic hydrolysis. − However, most studies remain at preliminary stages without in-depth identification and mechanistic elucidation of the bioactive peptides. Our previous studies have demonstrated that feather keratin fermentation using Bacillus licheniformis 8–4 yields feather keratin hydrolytic peptides with strong antioxidant activities in vitro . Using ultrafiltration, HPLC purification, and LC/MS-MS identification, two novel peptides, CRPCGPTP (CP-8) and ANSCNEPCVR (AR-10), were isolated and exhibited significant antioxidant activity.…”