Degradation of PrP<sup>Sc</sup>by Keratinolytic Protease from<i>Nocardiopsis</i>sp. TOA-1

Mitsuiki, Shinji; Zhao, Hui; Matsumoto, Daishi; Sakai, Masashi; Moriyama, Yasushi; Furukawa, Koichi; Kanouchi, Hiroaki; Oka, Tatsuzo

doi:10.1271/bbb.70.1246

Cited by 33 publications

(24 citation statements)

References 14 publications

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“…BA7, Actinomadura keratinilytica Cpt29 and Nocardiopsis sp. TOA-1 (Williams et al, 1990;Lin et al, 1992;Letourneau et al, 1998;Wang and Shih, 1999;Korkmaz et al, 2003;Gousterova et al, 2005;Mitsuiki et al, 2006;Yoshioka et al, 2007;Habbeche et al, 2014).…”

Section: Sources Of Keratinases Mesophilic Bacteriamentioning

confidence: 99%

“…Prions can cause transmissible spongiform encephalopathies of brain and nervous system including bovine spongiform encephalopathy, scrapie and Creutzfeldt-Jakob disease. Some bacterial and archaeal keratinases hydrolyze not only the hard-degrading keratinous fiber but also digest the protease resistant aggregated prion proteins (Mitsuiki et al, 2006;Šnajder et al, 2012;Suzuki et al, 2006;Gupta et al, 2013). Keratinase from strain PWD-1, a serine protease of a moderate thermophile Bacillus licheniformis (Lin et al, 1992) was the first reported protease capable of degrading the prions.…”

Section: Bio-safety On Infectious Prion Proteinsmentioning

confidence: 99%

“…Keratin and keratinase as well as keratinolytic microorganisms have tremendous applications in various sectors including biodegradation and waste management, biotechnology and industry, cosmetic and pharmaceutical products and medical treatments (Mitsuiki et al, 2006;Šnajder et al, 2012;Suzuki et al, 2006;Gupta et al, 2013). This review presents keratinase producing microorganisms with an emphasis on thermophiles.…”

Section: Introductionmentioning

confidence: 99%

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A Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine Proteases

Kanoksilapatham¹,

Intagun²

2017

American Journal of Applied Sciences

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Keratins are hard-degrading fibrous proteins, insoluble in water and organic solvents, often accumulated in nature and major components in feathers, skins, hair, horn, nail, hoof etc., Keratin-degrading microorganisms such as bacteria, archaea, actinomycetes and fungi employ keratinases to attack keratin. Keratinases belonging to subtilisin-like serine proteases were classified based on similarity of amino acid sequences. Keratinolytic thermophilic or hyperthermophilic bacteria and archaea have been known to degrade keratin at ≥70°C. General properties of thermozymes such as stability to heat and resistance to denaturing conditions; e.g., solvents and detergents have drawn attention to various biotechnological industries. Some bacterial and archaeal keratinases degrade not only fibrous keratin but also digest recalcitrant prion proteins, an etiologic agent of spongiform encephalopathies of brain and nervous system. Keratin and keratinase have a number of applications in various sectors, i.e., biotechnology, cosmetic and pharmaceutical industries, medical therapy and waste management. On the other hand, accumulation of excess amount of keratin is recognized as solid waste and troublesome environmental pollutant. Biodegradation involving either keratinolytic thermophiles or thermostable keratinases not only improve digestibility and nutritive values of keratinous meals (for mixers in animal feed stuffs), but also minimize risk from infection and microbial toxin transmitted to livestock.

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Section: Sources Of Keratinases Mesophilic Bacteriamentioning

confidence: 99%

Section: Bio-safety On Infectious Prion Proteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine Proteases

Kanoksilapatham¹,

Intagun²

2017

American Journal of Applied Sciences

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“…TOA-1 and has been demonstrated to degrade synthetic keratin substrate (Mitsuiki et al 2004), as well as scrapie prion (Mitsuiki et al 2006).…”

Section: Sources Of Microbial Keratinasesmentioning

confidence: 99%

Microbial keratinases: characteristics, biotechnological applications and potential.

Purchase

2016

The Handbook of Microbial Bioresources

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Keratinases are a group of proteolytic enzymes that can catalyse the cleavage and hydrolysis of the highly stable and fibrous proteins: keratins. A diverse range of microorganisms, including fungi, actinomycetes and bacteria, have been reported to produce keratinases that have biotechnological applications and potential. These keratinases have been usefully applied in agricultural, pharmaceutical, leather and textile processes as well as within environmentally friendly waste management solutions. Potential uses of keratinases include the fields of biomedicine, cosmetics, biological control and the generation of green energy. Herein we aim to provide an overview of the properties of this group of versatile enzymes, including the mechanisms of keratin degradation. The diversity of microbial sources of keratinases is discussed and the optimisation of keratianse production examined.We conclude with an assessment of the established biotechnological applications of keratinases in different industries and current research that highlights other promising potential uses.

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“…Protease digestion and elimination of ELISA or Western-blot immunoreactivity has been shown under a variety of conditions (Hui et al, 2004a(Hui et al, , 2004bLangeveld et al, 2003;Tsiroulnikov et al, 2004;Mitsuiki et al, 2006;Rapp et al, 2006;Scherbel et al, 2006;Muller-Hellwig et al, 2006). However, protease destruction of prions below in vitro assay detection limits does not necessarily mean that PrP res has been reduced to levels that are no longer infectious in more sensitive bioassays; therefore, methods investigating decontamination of infectious prions need to be tested in vivo until better in vitro methods are developed and validated (McLeod et al, 2004;Lawson et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Feasibility of infectious prion digestion using mild conditions and commercial subtilisin

Pilon

Nash²,

Arver³

et al. 2009

Journal of Virological Methods

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a b s t r a c tTwo serine protease enzymes, subtilisin 309 and subtilisin 309-v, were used to digest brain homogenates containing high levels of prion infectivity using mildly alkaline conditions to investigate prion decontamination methods. To establish that PrP res infectivity was eliminated, we utilized the Rocky Mountain Laboratory (RML) mouse-adapted scrapie model system for bioassay. Only one digestion condition (subtilisin 309 at 138 mAU/ml, 55• C and 14 h digestion time pH 7.9) was considered to be highly relevant statistically (P < 0.001) compared to control, with 52% of challenged mice surviving until the end of the study period. In contrast, treatment of PrP res by autoclaving at 134• C or treatment with hypochlorite at a concentration of 20,000 ppm completely protected mice from prionosis. Further, in vitro assays suggest that potential proteolytic based PrP res decontamination methods must use high enzyme concentration, pH values >9.0, and elevated temperatures to be a safely efficacious, thereby limiting applicability on delicate surgical instruments and use in the environment.Published by Elsevier B.V.

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Degradation of PrP^Scby Keratinolytic Protease fromNocardiopsissp. TOA-1

Abstract: A keratinolytic alkaline proteae (NAPase) from Nocardiopsis sp. TOA-1 degraded a scrapie prion without any chemical or physical treatment. Optimal temperature and pH were 60 degrees C and above pH 10.0. The scrapie prion was completely degraded within 3 min under optimal conditions.

Cited by 33 publications

References 14 publications

A Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine Proteases

A Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine Proteases

Microbial keratinases: characteristics, biotechnological applications and potential.

Feasibility of infectious prion digestion using mild conditions and commercial subtilisin

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Degradation of PrPScby Keratinolytic Protease fromNocardiopsissp. TOA-1

Abstract: A keratinolytic alkaline proteae (NAPase) from Nocardiopsis sp. TOA-1 degraded a scrapie prion without any chemical or physical treatment. Optimal temperature and pH were 60 degrees C and above pH 10.0. The scrapie prion was completely degraded within 3 min under optimal conditions.

Cited by 33 publications

References 14 publications

A Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine Proteases

A Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine Proteases

Microbial keratinases: characteristics, biotechnological applications and potential.

Feasibility of infectious prion digestion using mild conditions and commercial subtilisin

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Degradation of PrP^Scby Keratinolytic Protease fromNocardiopsissp. TOA-1