Fluorescence-based Quantification of Bioactive Keratin Peptides from Feathers for Optimizing Large-scale Anaerobic Fermentation and Purification

Jin, Hyeon Su; Park, Seon Yeong; Kim, Ji Yeon; Lee, Jae Eun; Lee, Han Seung; Kang, Nam Joo; Lee, Dong Woo

doi:10.1007/s12257-018-0400-8

Cited by 7 publications

(5 citation statements)

References 29 publications

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“…Although feathers, which are mainly composed of keratin, are potentially useful protein resources for bioactive peptides, rare amino acids, animal feeds and fertilizers (Papadopoulos et al, 1986;Onifade et al, 1998;Gupta and Ramnani, 2006;Jin et al, 2018), their structural rigidity limits their usefulness due to their strong resistance to proteolysis (Parry and North, 1998;Kreplak et al, 2004). The use of keratinases (or microorganisms) as biocatalysts for agricultural and environmental waste treatment to develop environmental recycling technologies for treating keratin-rich solid waste (Nam et al, 2002;Sharma and Devi, 2018;Yeo et al, 2018;Jin et al, 2019), as well as elucidating the molecular basis of keratin degradation, is especially interesting (Brandelli, 2008). Accordingly, there have been many attempts to identify microbial keratinases due to their attractiveness as tools for the pharmaceutical and cosmetic industries as well as for sustainable waste treatment (Brandelli, 2008;Brandelli et al, 2010;Jin et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Identification of keratinases from Fervidobacterium islandicum AW‐1 using dynamic gene expression profiling

Kang

Jin

et al. 2019

Microbial Biotechnology

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Summary Keratin degradation is of great interest for converting agro‐industrial waste into bioactive peptides and is directly relevant for understanding the pathogenesis of superficial infections caused by dermatophytes. However, the mechanism of this process remains unclear. Here, we obtained the complete genome sequence of a feather‐degrading, extremely thermophilic bacterium, Fervidobacterium islandicum AW‐1 and performed bioinformatics‐based functional annotation. Reverse transcription PCR revealed that 57 putative protease‐encoding genes were differentially expressed in substrate‐dependent manners. Consequently, 16 candidate genes were highly expressed under starvation conditions, when keratin degradation begun. Subsequently, the dynamic expression profiles of these 16 selected genes in response to feathers, as determined via quantitative real‐time PCR, suggested that they included four metalloproteases and two peptidases including an ATP‐dependent serine protease, all of which might act as key players in feather decomposition. Furthermore, in vitro keratinolytic assays supported the notion that recombinant enzymes enhanced the decomposition of feathers in the presence of cell extracts. Therefore, our genome‐based systematic and dynamic expression profiling demonstrated that these identified metalloproteases together with two additional peptidases might be primarily associated with the decomposition of native feathers, suggesting that keratin degradation can be achieved via non‐canonical catalysis of several membrane‐associated metalloproteases in cooperation with cytosolic proteases.

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Section: Introductionmentioning

confidence: 99%

Identification of keratinases from Fervidobacterium islandicum AW‐1 using dynamic gene expression profiling

Kang

Jin

et al. 2019

Microbial Biotechnology

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“…Keratin-derived bioactive peptides have been reported in the literature. These peptides have a range of activities like antimicrobial [149], antihypertensive [150], anti-inflammatory [151][152][153][154], antioxidant [149,150,155], inhibition of early stage amyloid aggregation [156], antidiabetic [157] or anti-aging [158][159][160] depending on the keratin source and the method of preparation. Producing protein feed supplements with antioxidant or anti-inflammatory properties as well as skin and hair products with antioxidant, anti-inflammatory, antimicrobial or anti-aging properties would most likely increase the value of these products.…”

Section: Potential Applications Of Keratinasesmentioning

confidence: 99%

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

et al. 2020

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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 ...

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“…The molecular structure has to be converted to smaller digestible proteins. Some industrial-scale processes have already been developed: thermal pressure hydrolysis (TPH) optionally in combination with extrusion, chemical hydrolysis, or enzymatic/fermented hydrolysis. , …”

Section: Introductionmentioning

confidence: 99%

“…Some industrial-scale processes have already been developed: 9 thermal pressure hydrolysis (TPH) 10 optionally in combination with extrusion, 11 chemical hydrolysis, 12 or enzymatic/fermented hydrolysis. 13,14 TPH is the most common industrial method currently in use. Earlier work has described the effect of temperature (120−160 °C) and time (10 and 30 min) during TPH on AEH, 15 showing four different "stages" characterized by the temperature.…”

Section: ■ Introductionmentioning

confidence: 99%

Fourier Transform Infrared Spectroscopy for Assessing Structural and Enzymatic Reactivity Changes Induced during Feather Hydrolysis

Windt

Scott

Seeger³

et al. 2022

ACS Omega

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Chicken feathers are major byproducts of the livestock processing industry with high potential in the feed sector. In this study, we present a new approach using Fourier transform infrared (FTIR) spectroscopy to detect the structural changes of feather keratin and its availability for enzymatic hydrolysis (AEH) induced by the thermal pressure hydrolysis (TPH) process. Compared to time-consuming in vitro measurement techniques, the proposed method provides rapid information about the structural changes during TPH which enables quick adaptation of TPH conditions as the quality of the incoming feather changes. By analyzing the FTIR spectra of raw and processed feathers, it was found that AEH negatively relates to the β-sheet content (represented by two IR peaks centered at 1635 and 1689 cm–1), while it positively relates to a new series of peaks centered around 1700 cm–1 appearing after the TPH process. The proposed FTIR technique provides a reliable and rapid approach to determine the digestibility indicated by AEH of the processed feather and may be used in process control and optimization.

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Fluorescence-based Quantification of Bioactive Keratin Peptides from Feathers for Optimizing Large-scale Anaerobic Fermentation and Purification

Cited by 7 publications

References 29 publications

Identification of keratinases from Fervidobacterium islandicum AW‐1 using dynamic gene expression profiling

Identification of keratinases from Fervidobacterium islandicum AW‐1 using dynamic gene expression profiling

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

Fourier Transform Infrared Spectroscopy for Assessing Structural and Enzymatic Reactivity Changes Induced during Feather Hydrolysis

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