Improved microbial degradation of animal hair waste from leather industry using Brevibacterium luteolum (MTCC 5982)

Thankaswamy, Shiny Renitha; Sundaramoorthy, Sundarapandiyan; Palanivel, Saravanan; Ramudu, Kamini Numbi

doi:10.1016/j.jclepro.2018.04.095

“…AS-S10-11 [54]. Although, temperature optimums vary from 30 • C for the keratinase from Brevibacterium luteolum [55] to 100 • C for the keratinase from Fervidobacterium islandicum AW-1 [56].…”

Section: Microbial Degradation Of Keratinmentioning

confidence: 99%

“…However, the number of Bacillus strains with keratinolytic activity prevailed over any other genus of bacteria . Valorisation of waste feathers [5,65,66,87] and the replacement of the traditional, highly polluting hide dehairing step used in the leather industry with a more environmentally friendly enzymatic step using keratinases [2,55,79,88] were the dominant themes of these papers.…”

Section: Microbial Degradation Of Keratinmentioning

confidence: 99%

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

Martìnez

¹

,

Cai

²

,

Nachtschatt

³

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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“…Keratinases (EC 3.4.21/24/99.11) are a class of proteases that hydrolyze keratin, an advantage over other proteases (Brandelli, Daroit and Riffel 2010;Gegeckas et al 2018). These enzymes have applications such as biotechnology (Okoroma et al 2012;Mazotto et al 2013; Paul et al 2014; Brandelli, Sala and Kalil 2015) and waste degradation (Fang et al 2013a;Yusuf et al 2016;Su et al 2017;Abdel-Fattah et al 2018;Thankaswamy et al 2018).…”

Section: Introduction Highlightsmentioning

confidence: 99%

Reactional Ultrasonic Systems And Microwave Irradiation For Pretreatment Of Agro-Industrial Waste To Increase Enzymatic Activity

Czapela

¹

,

Kubeneck

²

,

Preczeski

³

et al. 2020

Preprint

1

0

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Pretreatment of keratinous residues using an ultrasonic reaction system provides greater enzymatic production in less time. This is a promising technology for measuring enzyme activity and microwave processes. In the present work, an ultrasonic probe reaction system was used to evaluate the potential of swine hair pretreatment. The pretreated material was submerged with non-pretreated residues for 9 days to obtain the enzyme. Enzyme activity was measured in the extracts obtained using the ultrasonic probe, ultrasonic bath, and microwave. We also used the enzymatic concentration technique with NaCl and acetone. Homemade enzymatic extracts were evaluated for their ability to degrade swine hair and chicken feathers by comparing them with the activities commercial enzymes. Macrobeads gave greater energy dissipation in less time, providing greater enzyme activity (50.8 U/mL over 3 days). In terms of waste degradation, non-pretreated swine hair was more promising. The ultrasonic probe reaction system had the potential to evaluate increased enzyme activity (38.4% relative activity) and the enzyme concentration increased activity by 53.5%. The homemade enzymatic extract showed promise for degradation of keratinous residues.

show abstract

“…Keratinases (EC 3.4.21/24/99.11) are a class of proteases that hydrolyze keratin, an advantage over other proteases (Brandelli, Daroit and Riffel 2010;Gegeckas et al 2018). These enzymes have applications such as biotechnology (Okoroma et al 2012;Mazotto et al 2013;Paul et al 2014;Brandelli, Sala and Kalil 2015) and waste degradation (Fang et al 2013a;Yusuf et al 2016;Su et al 2017;Abdel-Fattah et al 2018;Thankaswamy et al 2018). They can be obtained commercially or from submerged fermentation (FS) or solid-state fermentation (FES) through microorganisms (Mazotto et al 2013) such as fungi (Kushwaha 1983;Santos et al 1996), that are considered good producers of keratinases; they can also be isolated from keratinous waste disposal sites (Kaul and Sumbali 1997;Riffel and Brandelli 2006).…”

Section: Introductionmentioning

confidence: 99%

Reactional Ultrasonic Systems and Microwave Irradiation For Pretreatment Of Agro-Industrial Waste To Increase Enzymatic Activity

Czapela

¹

,

Kubeneck

²

,

Preczeski

³

et al. 2020

Preprint

0

View full text Add to dashboard Cite

Pretreatment of keratinous residues using an ultrasonic reaction system provides greater enzymatic production in less time. This is a promising technology for measuring enzyme activity and microwave processes. In the present work, an ultrasonic probe reaction system was used to evaluate the potential of swine hair pretreatment. The pretreated material was submerged with non-pretreated residues for 9 days to obtain the enzyme. Enzyme activity was measured in the extracts obtained using the ultrasonic probe, ultrasonic bath, and microwave. We also used the enzymatic concentration technique with NaCl and acetone. Homemade enzymatic extracts were evaluated for their ability to degrade swine hair and chicken feathers by comparing them with the activities commercial enzymes. Macrobeads gave greater energy dissipation in less time, providing greater enzyme activity (50.8 U/mL over 3 days). In terms of waste degradation, non-pretreated swine hair was more promising. The ultrasonic probe reaction system had the potential to evaluate increased enzyme activity (38.4% relative activity) and the enzyme concentration increased activity by 53.5%. The homemade enzymatic extract showed promise for degradation of keratinous residues.

show abstract

Improved microbial degradation of animal hair waste from leather industry using Brevibacterium luteolum (MTCC 5982)

Cited by 45 publications

References 30 publications

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

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

Reactional Ultrasonic Systems And Microwave Irradiation For Pretreatment Of Agro-Industrial Waste To Increase Enzymatic Activity

Reactional Ultrasonic Systems and Microwave Irradiation For Pretreatment Of Agro-Industrial Waste To Increase Enzymatic Activity

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