Using a keratinase to degrade chicken feathers for improved extraction of glucocorticoids

Alba, Andrew C.; Strauch, T. A.; Keisler, D.H.; Wells, Kevin D.; Kesler, Dylan C.

doi:10.1016/j.ygcen.2018.10.002

Cited by 17 publications

(27 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Consequently, keratinase from Bacillus sp. C4 promoted the extraction of glucocorticoids from chicken feather biomass (Alba et al, 2019). The efficiency of the enzymatic method was further confirmed by conducting parallelism test and hormone recovery employing radioimmunoassay.…”

Section: Other Potential Keratinase Applicationsmentioning

confidence: 85%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

View full text Add to dashboard Cite

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.

show abstract

Section: Other Potential Keratinase Applicationsmentioning

confidence: 85%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

View full text Add to dashboard Cite

show abstract

“…In laying hens, the condition of the plumage and the integument acts as an indicator for feather pecking and cannibalism, both being behavioral disorders caused by various challenges the birds had or have to cope with ( Sepeur et al., 2015 ; Giersberg et al., 2017 ). Recent studies showed that the evaluation of animal welfare in birds may be carried out objectively and noninvasively with the measurement of the stress-related hormone corticosterone in feathers ( Bortolotti et al., 2008 ; Bortolotti et al., 2009 ; Fairhurst et al., 2011 ; Carbajal et al., 2014 ; Ganz et al., 2018 ; Johns et al., 2018 ; Weimer et al., 2018 ; Alba et al., 2019 ; von Eugen et al., 2019 ; Nordquist et al., 2020 ).…”

Section: Introductionmentioning

confidence: 99%

“…Subsequent studies on corticosterone in feathers were performed mostly in wild birds (e.g., Bortolotti et al., 2009 ; Koren et al., 2011 ; Lattin et al., 2011 ; Fairhurst et al., 2012 ; Lendvai et al., 2013 ; Harms et al., 2015 ; Kouwenberg et al., 2016 ; Aharon-Rotman et al., 2017 ; Freeman and Newman, 2018 ; Monclús et al., 2020 ), using feather corticosterone as a retrospective view on challenges the birds had to cope with during feather growth. Despite the wild birds, results of first investigations in poultry ( Berkvens, 2012 ; Carbajal et al., 2014 ; Jenni-Eiermann et al., 2015 ; Zeinstra et al., 2015 ; Johns et al., 2017 ; Weimer et al., 2018 ; Alba et al., 2019 ; von Eugen et al., 2019 ; Nordquist et al., 2020 ; Lindenwald and Rautenschlein, unpublished data) are also encouraging; however, in the absence of a standardized procedure, authors applied different methods to detect and quantify corticosterone in feathers. These variations, such as variations in the amount of feather material or methanol volume for the extraction, crushed vs. grind up feathers, and different methods for filtration or different assays, make it rather impossible to compare the results, properly ( Romero and Fairhurst, 2016 ).…”

Section: Introductionmentioning

confidence: 99%

“…This is essential, given that, to the best of our knowledge, no proper validation for commercial laying hens has been performed before and, especially, because noninvasive measurements of corticosterone and related hormones are finding their way into field studies, applied by researchers being new in the field of noninvasive endocrine assessments ( Buchanan and Goldsmith, 2004 ). Alba et al. (2019) validated another method for domestic chickens, using a keratinase to digest the protein matrix in the first step.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Corticosterone in feathers of laying hens: an assay validation for evidence-based assessment of animal welfare

et al. 2020

View full text Add to dashboard Cite

Studies indicate that the evaluation of animal welfare in birds may be carried out with the measurement of the stress-related hormone corticosterone in feathers. However a standardized procedure for corticosterone measurements in feathers is lacking, a validation needs to be carried out for each new species before implementation. The aim of the present study was to establish a valid method to measure corticosterone concentrations in feathers of laying hens in a precise and repeatable manner using an established and commercially available ELISA. Validation was performed with feather pools of tail and interscapular feathers of commercial Lohmann Brown laying hens. Assessment groups, consisting of 5 replicates, were created. All replicates of an assessment group were processed at the same time. Each replicate was run in 4 repetitions by ELISA. Intra-assay and interassay CV was 7.5 and 6.4%, respectively. The serial dilution showed linearity and parallelism. Examining the hormone extraction efficiency by using different methanol volumes resulted in no statistical differences ( P > 0.05). Pulverized feathers showed higher corticosterone values than minced feathers ( P > 0.05). Differences were shown between 2 feather types (tail vs. interscapular feathers; P < 0.05), as well as between vane and rachis ( P < 0.05). Performance of a freeze–thaw cycle led to a decrease of corticosterone concentrations in the samples. A possible effect of UV-A radiation on the stability of corticosterone in the feathers was not found ( P > 0.05). With the present study, a valid protocol, feasible for analyzing feather pools of laying hens, was developed. It may provide fundamentals for further investigations on corticosterone in feathers as a noninvasive indicator to evaluate aspects of animal welfare.

show abstract

“…There are also a number of promising applications of keratinases that have not been commercialized to date: dag or manure balls removal from cattle hides and tails [145]; extraction of glucocorticoids from chicken feathers to monitor the stress level in poultry breeding and production programmes [146] extraction of chicken feather cholesterol as a precursor to bile salts that can be used to produce bio-emulsifiers and biosurfactants in the cosmetic industry [18]; selective hydrolysis of wool from wool/polyester or mixed textiles to facilitate textile recycling [147]; and dehairing of hides in the leather industry [64,65,82].…”

Section: Potential Applications Of Keratinasesmentioning

confidence: 99%

Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production

et al. 2020

View full text Add to dashboard Cite

Keratins are important structural proteins produced by mammals, birds and reptiles. Keratins usually act as a protective barrier or a mechanical support. Millions of tonnes of keratin wastes and low value co-products are generated every year in the poultry, meat processing, leather and wool industries. Keratinases are proteases able to breakdown keratin providing a unique opportunity of hydrolysing keratin materials like mammalian hair, wool and feathers under mild conditions. These mild conditions ameliorate the problem of unwanted amino acid modification that usually occurs with thermochemical alternatives. Keratinase hydrolysis addresses the waste problem by producing valuable peptide mixes. Identifying keratinases is an inherent problem associated with the search for new enzymes due to the challenge of predicting protease substrate specificity. Here, we present a comprehensive review of twenty sequenced peptidases with keratinolytic activity from the serine protease and metalloprotease families. The review compares their biochemical activities and highlights the difficulties associated with the interpretation of these data. Potential applications of keratinases and keratin hydrolysates generated with these enzymes are also discussed. The review concludes with a critical discussion of the need for standardized assays and increased number of sequenced keratinases, which would allow a meaningful comparison of the biochemical traits, phylogeny and keratinase sequences. This deeper understanding would facilitate the search of the vast peptidase family sequence space for novel keratinases with industrial potential.Catalysts 2020, 10, 184 2 of 23 with keratinolytic activity for keratin hydrolysis protects the integrity of the keratin amino acids in most cases and allows control over the peptide size in the hydrolysate that is not readily achievable with other methods [5]. This degree of control allows the production of bespoke medical biomaterials, smart biocomposites, protein feed supplements with enhanced nutritional and bioactive properties as well as personal care products with enhanced functional and bioactive properties.Identifying peptidases with keratinolytic activity is an inherent problem associated with the search for new enzymes. Keratinase activity however appears to be dependent on the accessibility of the keratin substrate to the enzyme [6,7]. Thermochemical or biochemical treatment of the keratin, with emphasis on the reduction of the disulphide bond and disruption of other important bonds involved in the structural stability of keratin like isopeptide, hydrogen and glycolytic bonds [6,[8][9][10], appears to be the prerequisite for enzymatic hydrolysis. Sulphitolysis, which involves reduction of the disulphide bond in keratin, often acts synergistically with keratinases in nature [6,7]. Although destabilization of the keratin structure is a prerequisite for keratin hydrolysis, not all peptidases can hydrolyse keratin. Peptidases like trypsin, papain and pepsin cannot hydrolyse keratin as efficiently ...

show abstract

Using a keratinase to degrade chicken feathers for improved extraction of glucocorticoids

Cited by 17 publications

References 31 publications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Corticosterone in feathers of laying hens: an assay validation for evidence-based assessment of animal welfare

Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production

Contact Info

Product

Resources

About