Draft Genome Sequence of Meiothermus ruber H328, Which Degrades Chicken Feathers, and Identification of Proteases and Peptidases Responsible for Degradation

Inada, Shuhei; Watanabe, Kunihiko

doi:10.1128/genomea.00176-13

Cited by 18 publications

(17 citation statements)

References 7 publications

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“…Phyla-AMPHORA ( 6 ) and manual BLASTp searches identified 508 of 517 Deinococcus - Thermus -specific phylogenetic marker genes. This suggests that the draft genome is >90% complete and that the genome is comparable in size to that of other M. ruber genomes (3.03 to 3.10 Mb [ 5 , 7 ]).…”

Section: Genome Announcementmentioning

confidence: 83%

Draft Genome Sequence of the Deinococcus-Thermus Bacterium Meiothermus ruber Strain A

et al. 2015

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Section: Genome Announcementmentioning

confidence: 83%

Draft Genome Sequence of the Deinococcus-Thermus Bacterium Meiothermus ruber Strain A

et al. 2015

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“…The disulphide bonds are cleaved first, and the keratin is denatured, giving easy access for keratinases to degrade the keratin protein even further . Many other experimental studies provided evidence that disulphide reductase and the intracellular enzyme cysteine dioxygenase can break down sulphur bridges, and lead to production and secretion of sulphite, thus giving the enzymes improved access to the keratinaceous substrate . For this reason, molecular or genetic studies in vitro are unable to examine comprehensively the extent of keratin degradation by clinical isolates of dermatophytes, and the range of animal hosts attacked by the pathogen cannot be assessed.…”

Section: Discussionmentioning

confidence: 99%

“…41,48,51 On the other hand, it is widely agreed that keratin breakdown requires more than just one enzyme. 22,41,51,53,54 This concept was developed from observations that the keratinase activity of a culture broth was not detected after purified keratinase active protein was added, which indicated at least two enzymes working synergistically together in decomposition. 22,53,55 The average standard deviation (SD) values are given in brackets.…”

Section: Discussionmentioning

confidence: 99%

The host range of dermatophytes, it is at all possible? Phenotypic evaluation of the keratinolytic activity of Trichophyton verrucosum clinical isolates

Gnat

Łagowski

Nowakiewicz

et al. 2019

Mycoses

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Summary Dermatophytes are fungi that have an ability to invade keratinised structures. Enzymes secreted by dermatophytes can underlie fungal survival on the host and development of infection. It is possible that the range of activity of keratinases from various dermatophytes is limited to specific species of animals and groups of people. The aim of this study was to carry out phenotypic analysis of the degree of keratinolytic activity of Trichophyton verrucosum strains using hairs of humans and various animal species as substrates. Our results indicated that the activity of keratinases is substrate‐induced. The host range of T. verrucosum can be defined as wide. The highest activity of keratinases was recorded in media containing keratin from cow (Bos taurus) and sheep (Ovis aries) hairs in comparison with that from other tested species. The production of keratin‐degrading enzymes is a function of time, with the peak of their activity occurring on day 15 of incubation. The role of keratin‐degrading enzymes in the pathogenesis of dermatophytosis is becoming increasingly clearer. Given the conceptual understanding that keratin breakdown may require more than just one enzyme, the use of phenotypic methods is an optimal approach to in vitro study of the decomposition of species‐specific keratin.

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“…In the last one to two decades, the DNA and RNA approach has also been brought in use, first through an EST, expressed sequence tag methodological approach. Only a few articles describe work that has taken full advantage of the options available to rapidly gain increased insight into keratinases through use of explorative and comparative genomics, transcriptomics and mass spectrometry (MS)/proteomics (Huang et al 2015a ; Inada and Watanabe 2013 ; Lange et al 2014 ; Park et al 2014 ; Yong et al 2013 ). It is to be expected that progress in understanding the molecular structure of a potentially valuable polymer such as keratin will be gained soon, due to increased attention to the need for improved resource efficiency.…”

Section: Introductionmentioning

confidence: 99%

Microbial decomposition of keratin in nature—a new hypothesis of industrial relevance

Lange

Huang

Busk

2016

Appl Microbiol Biotechnol

226

181

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Discovery of keratin-degrading enzymes from fungi and bacteria has primarily focused on finding one protease with efficient keratinase activity. Recently, an investigation was conducted of all keratinases secreted from a fungus known to grow on keratinaceous materials, such as feather, horn, and hooves. The study demonstrated that a minimum of three keratinases is needed to break down keratin, an endo-acting, an exo-acting, and an oligopeptide-acting keratinase. Further, several studies have documented that disruption of sulfur bridges of the keratin structure acts synergistically with the keratinases to loosen the molecular structure, thus giving the enzymes access to their substrate, the protein structure. With such complexity, it is relevant to compare microbial keratin decomposition with the microbial decomposition of well-studied polymers such as cellulose and chitin. Interestingly, it was recently shown that the specialized enzymes, lytic polysaccharide monoxygenases (LPMOs), shown to be important for breaking the recalcitrance of cellulose and chitin, are also found in keratin-degrading fungi. A holistic view of the complex molecular self-assembling structure of keratin and knowledge about enzymatic and boosting factors needed for keratin breakdown have been used to formulate a hypothesis for mode of action of the LPMOs in keratin decomposition and for a model for degradation of keratin in nature. Testing such hypotheses and models still needs to be done. Even now, the hypothesis can serve as an inspiration for designing industrial processes for keratin decomposition for conversion of unexploited waste streams, chicken feather, and pig bristles into bioaccessible animal feed.

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Draft Genome Sequence of Meiothermus ruber H328, Which Degrades Chicken Feathers, and Identification of Proteases and Peptidases Responsible for Degradation

Cited by 18 publications

References 7 publications

Draft Genome Sequence of the Deinococcus-Thermus Bacterium Meiothermus ruber Strain A

Draft Genome Sequence of the Deinococcus-Thermus Bacterium Meiothermus ruber Strain A

The host range of dermatophytes, it is at all possible? Phenotypic evaluation of the keratinolytic activity of Trichophyton verrucosum clinical isolates

Microbial decomposition of keratin in nature—a new hypothesis of industrial relevance

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