Iron containing keratinolytic metallo-protease produced by Chryseobacterium gleum

Chaudhari, Priti N.; Chaudhari, Bhushan L.; Chincholkar, S. B.

doi:10.1016/j.procbio.2012.11.009

Cited by 25 publications

(11 citation statements)

References 39 publications

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“…Keratinases/keratinolytic microorganisms have, for instance, been in use for the production of feather-meal, the enhancement of drug delivery, the hydrolysis of prion, the construction of biodegradable films, and the production of biofuels [7]. They have been purified from diverse microorganisms, including fungi, such as Purpureocillium lilacinum LPS # 876 [8] and Chryseobacterium gelum [9], and bacteria, such as Streptomyces [10] and Bacillus [11], [12]. In fact, several serine peptidases have so far been isolated, purified and characterized from various species, including B. pumilus CBS [13], B. subtilis [14], and B. circulans DZ100 [15].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and Molecular Characterization of a Serine Keratinase from Brevibacillus brevis US575 with Promising Keratin-Biodegradation and Hide-Dehairing Activities

et al. 2013

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Dehairing is one of the highly polluting operations in the leather industry. The conventional lime-sulfide process used for dehairing produces large amounts of sulfide, which poses serious toxicity and disposal problems. This operation also involves hair destruction, a process that leads to increased chemical oxygen demand (COD), biological oxygen demand (BOD), and total suspended solid (TSS) loads in the effluent. With these concerns in mind, enzyme-assisted dehairing has often been proposed as an alternative method. The main enzyme preparations so far used involved keratinases. The present paper reports on the purification of an extracellular keratinase (KERUS) newly isolated from Brevibacillus brevis strain US575. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme was a monomer with a molecular mass of 29121.11 Da. The sequence of the 27 N-terminal residues of KERUS showed high homology with those of Bacillus keratinases. Optimal activity was achieved at pH 8 and 40°C. Its thermoactivity and thermostability were upgraded in the presence of 5 mM Ca2+. The enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP), which suggests that it belongs to the serine protease family. KERUS displayed higher levels of hydrolysis, substrate specificity, and catalytic efficiency than NUE 12 MG and KOROPON® MK EG keratinases. The enzyme also exhibited powerful keratinolytic activity that made it able to accomplish the entire feather-biodegradation process on its own. The kerUS gene encoding KERUS was cloned, sequenced, and expressed in Escherichia coli. The biochemical properties of the extracellular purified recombinant enzyme (rKERUS) were similar to those of native KERUS. Overall, the findings provide strong support for the potential candidacy of this enzyme as an effective and eco-friendly alternative to the conventional chemicals used for the dehairing of rabbit, goat, sheep and bovine hides in the leather processing industry.

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Section: Introductionmentioning

confidence: 99%

Biochemical and Molecular Characterization of a Serine Keratinase from Brevibacillus brevis US575 with Promising Keratin-Biodegradation and Hide-Dehairing Activities

et al. 2013

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“…This property of the enzyme proved the role of Fe 2+ ions as cofactor of this enzyme. Fe‐metalloproteases were also reported for Aeromonas caviae and Chryseobacterium gleum . The inhibitory effect of some metal ions may be due to attachment with SH groups of Cys‐X breaking SS bridges thus changing the conformation of enzyme or may be due to the replacement with metals originally present in the enzyme structure …”

Section: Resultsmentioning

confidence: 88%

The biotechnological potential of subtilisin‐like fibrinolytic enzyme from a newly isolated Lactobacillus plantarum KSK‐II in blood destaining and antimicrobials

Kotb

2014

Biotechnology Progress

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An antimicrobial oxidative- and SDS-stable fibrinolytic alkaline protease designated as KSK-II was produced by Lactobacillus plantarum KSK-II isolated from kishk, a traditional Egyptian food. Maximum enzyme productivity was obtained in medium containing 1% lactose and 0.5% soybean flour as carbon and nitrogen sources, respectively. Purification of enzyme increased its specific activity to 1,140-fold with a recovery of 33% and molecular weight of 43.6 kDa. Enzyme activity was totally lost in the presence of ethylenediaminetetraacetic acid and was restored after addition of Fe(2+) suggesting that KSK-II is a metalloprotease and Fe(2+) acts as cofactor. Enzyme hydrolyzed not only the natural proteins but also synthetic substrates, particularly Suc-Ala-Ala-Pro-Phe-pNA. KSK-II can hydrolyze the Lys-X easier than Arg-X; thus, it was considered as a subtilisin-family protease. Its apparent Km , Vmax , and Kcat were 0.41 mM, 6.4 µmol mg(-1) min(-1) , and 28.0 s(-1) , respectively. KSK-II is industrially important from the perspectives of its maximal activity at 50°C (stable up to 70°C), ability to function at alkaline pH (10.0), stability at broad pH ranges (7.5-12.0) in addition to its stability toward SDS, H2 O2 , organic solvents, and detergents. We emphasize for the first time the potential of fibrinolytic activity for alkaline proteases used in detergents especially in blood destaining.

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“…3). Chryseobacterium strains often produce keratinases at mesophilic temperatures (Venter et al, 1999;Chaudhari et al, 2013). Although these conditions were considered satisfactory for Fig.…”

Section: Resultsmentioning

confidence: 99%

Isolation, Identification, and Characterization of a Keratin-degrading Bacterium Chryseobacterium sp. P1-3

Hong

Park

Jung

et al. 2015

JABC

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In this study, a keratin-degrading bacterium was isolated from soil contaminated with feather waste. The isolated strain was identified as Chryseobacterium sp. P1-3 on the basis of the 16S rRNA gene sequence alignment. Chryseobacterium sp. P1-3 is currently used in various biotechnological applications (e.g., in the hydrolysis of poultry feathers). It hydrolyzed the feather meal within 2 days and possesses a high level of keratinase activity (98 U/mL). The keratinase, partially purified from this strain, prefers casein as a substrate and shows optimal activity at a temperature of 30 o C and at a pH of 8.0.

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Iron containing keratinolytic metallo-protease produced by Chryseobacterium gleum

Cited by 25 publications

References 39 publications

Biochemical and Molecular Characterization of a Serine Keratinase from Brevibacillus brevis US575 with Promising Keratin-Biodegradation and Hide-Dehairing Activities

Biochemical and Molecular Characterization of a Serine Keratinase from Brevibacillus brevis US575 with Promising Keratin-Biodegradation and Hide-Dehairing Activities

The biotechnological potential of subtilisin‐like fibrinolytic enzyme from a newly isolated Lactobacillus plantarum KSK‐II in blood destaining and antimicrobials

Isolation, Identification, and Characterization of a Keratin-degrading Bacterium Chryseobacterium sp. P1-3

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