Purification and Some Properties of a Keratinolytic Enzyme from an Alkaliphilic<i>Nocardiopsis</i>sp. TOA-1

Mitsuiki, Shinji; Sakai, Masashi; Moriyama, Yasushi; Goto, Minoru; Furukawa, Koichi

doi:10.1271/bbb.66.164

Cited by 59 publications

(12 citation statements)

References 11 publications

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“…The purified keratinase effectively hydrolyzed native keratin in the presence of 2-mercaptoacetate. As shown by Mitsuiki et al (2002) , the alkaliphilic Nocardiopsis sp. TOA-1, grown on a skim milk/yeast extract medium, biosynthesized a highly stable keratinolytic enzyme with an optimum activity at pH 11.0–11.5 and temperature of 70–75 °C.…”

Section: Introductionmentioning

confidence: 91%

Keratinolytic abilities of <italic>Micrococcus luteus</italic> from poultry waste

Łaba¹,

Choińska²,

Rodziewicz³

et al. 2015

Braz. J. Microbiol.

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Keratinolytic microorganisms have become the subject of scientific interest due to their ability to biosynthesize specific keratinases and their prospective application in keratinic waste management. Among several bacterial classes, actinobacteria remain one of the most important sources of keratin-degrading strains, however members of the Micrococcaceae family are rarely scrutinized in regard to their applicatory keratinolytic potential. The tested Micrococcus sp. B1pz isolate from poultry feather waste was identified as M. luteus. The strain, grown in the medium with 1–2% chicken feathers and a yeast extract supplement, produced keratinases of 32 KU and lower level of proteases, 6 PU. It was capable to effectively decompose feathers or “soft” keratin of stratum corneum, in contrast to other “hard” hair-type keratins. The produced keratinolytic enzymes were mainly a combination of alkaline serine or thiol proteases, active at the optimum pH 9.4, 55 °C. Four main protease fractions of 62, 185, 139 and 229 kDa were identified in the crude culture fluid. The research on the auxiliary role of reducing factors revealed that reducing sulfur compounds could be applied in keratinolysis enhancement during enzymatic digestion of keratin, rather than in culture conditions. The presented M. luteus isolate exhibits a significant keratinolytic potential, which determines its feasible applicatory capacity towards biodegradation of poultry by-products or formulation of keratin-based feed components.

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Section: Introductionmentioning

confidence: 91%

Keratinolytic abilities of <italic>Micrococcus luteus</italic> from poultry waste

Łaba¹,

Choińska²,

Rodziewicz³

et al. 2015

Braz. J. Microbiol.

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“…Most of the keratinases known to date, have been classified as serine proteases [ 14 , 16 , 19 , 58 , 59 ], and a few as metalloproteases [ 20 , 60 , 61 ]. The latter mainly come from Gram-negative bacteria and fungi [ 62 ].…”

Section: Discussionmentioning

confidence: 99%

An Integrative Bioinformatic Analysis for Keratinase Detection in Marine-Derived Streptomyces

et al. 2021

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Keratinases present promising biotechnological applications, due to their ability to degrade keratin. Streptomyces appears as one of the main sources of these enzymes, but complete genome sequences of keratinolytic bacteria are still limited. This article reports the complete genomes of three marine-derived streptomycetes that show different levels of feather keratin degradation, with high (strain G11C), low (strain CHD11), and no (strain Vc74B-19) keratinolytic activity. A multi-step bioinformatics approach is described to explore genes encoding putative keratinases in these genomes. Despite their differential keratinolytic activity, multiplatform annotation reveals similar quantities of ORFs encoding putative proteases in strains G11C, CHD11, and Vc74B-19. Comparative genomics classified these putative proteases into 140 orthologous groups and 17 unassigned orthogroup peptidases belonging to strain G11C. Similar network analysis reveals three network communities of putative peptidases related to known keratinases of the peptidase families S01, S08, and M04. When combined with the prediction of cellular localization and phylogenetic reconstruction, seven putative keratinases from the highly keratinolytic strain Streptomyces sp. G11C are identified. To our knowledge, this is the first multi-step bioinformatics analysis that complements comparative genomics with phylogeny and cellular localization prediction, for the prediction of genes encoding putative keratinases in streptomycetes.

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“…Subtilisin-like proteases are generally bacterial in origin and secreted extracellularly for the purpose of scavenging nutrients [18][19][20][21]. They are highly sensitive towards phenyl methyl sulfonyl fluoride and diisopropylfluorophosphate, but not to chelating agents such as EDTA.…”

Section: Discussionmentioning

confidence: 99%

Development of a High-Throughput Diagnosis Method for Detecting the ALDH2 Gene Using Fingernail DNA

Takii¹

2013

Int. J. Biotech. Well. Indus.

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A clinical method for effective genetic screening of the aldehyde dehydrogenase 2 (ALDH2) gene was developed, using the fingernail as a source of DNA material. A highly effective protease that could solubilize fingernail keratin and inactivate any DNase co-existing in the tissue was obtained by cloning and sequencing the gene for alkaline protease from Bacillus alcalophilus, followed by expression of the gene in Bacillus subtilis. The amino acid sequence of MIB029 protease contained common regions found in four other subtilisin-like proteases. In the fingernails of 113 female university students (average age 20.8 ± 0.7 years; body mass index, 20.4 ±1.6), ALDH2 frequency was 0.66 for the typical Glu homozygote, 0.32 for the heterozygote (Glu487Lys), and 0.020 for the atypical Lys homozygote. Through a questionnaire, it was found that the subjects had not previously received information regarding the relationship between their genetic background and consumption of alcoholic beverages. We found that the genetic single nucleotide polymorphism (SNP) background to alcoholism can be easily detected by collecting fingernails, which is convenient for subjects or patients.

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Purification and Some Properties of a Keratinolytic Enzyme from an AlkaliphilicNocardiopsissp. TOA-1

Cited by 59 publications

References 11 publications

Keratinolytic abilities of <italic>Micrococcus luteus</italic> from poultry waste

Keratinolytic abilities of <italic>Micrococcus luteus</italic> from poultry waste

An Integrative Bioinformatic Analysis for Keratinase Detection in Marine-Derived Streptomyces

Development of a High-Throughput Diagnosis Method for Detecting the ALDH2 Gene Using Fingernail DNA

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