Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50

Elhoul, Mouna Ben; Jaouadi, Nadia Zaraî; Rekik, Hatem; Benmrad, Maroua Omrane; Mechri, Sondes; Moujehed, Emna; Kourdali, Sidali; Hattab, Mohamed El; Badis, Abdelmalek; Béjar, Samír; Jaouadi, Bassem

doi:10.1016/j.ijbiomac.2016.07.009

Cited by 43 publications

(28 citation statements)

References 74 publications

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“…Actinomadura rubrobrunea NBRC 15275 T and A. viridilutea IFO 14480 T were thermophilic species, yet their xylanolytic activities remain unknown. However, as reported by Elhoul et al (2016), A. viridilutea was also a potential producer of keratinase.…”

Section: Phylogenetic Tree Analysessupporting

confidence: 58%

Xylan-degrading ability of thermophilic Actinobacteria from soil in a geothermal area

Rachmania¹,

Ningsih²,

Setyaningsih³

et al. 2019

Biodiversitas

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Abstract. Rachmania MK, Ningsih F, Setyaningsih PP, Syafitri WA, Sari DCAF, Yabe S, Yokota A, Oetari A, Sjamsuridjal W. 2020. Xylan-degrading ability of thermophilic Actinobacteria isolated from soil in a geothermal area. Biodiversitas 21: 144-154. This study was conducted to obtain the potential isolates of xylan-degrading thermophilic Actinobacteria. Seventeen isolates were obtained from the soil samples collected from Cisolok geysers in West Java, Indonesia. These isolates were screened for their xylan-degrading ability on minimal medium with the addition of 0.5% xylan as substrate, and were incubated at various temperatures for 7 days. A total of 15, 14, 4, and 3 isolates showed a xylan-degrading ability at 45°C, 50°C, 55°C, and 60°C, respectively. The three isolates (SL1-2-R-2, SL1-2-R-3, and SL1-2-R-4) that showed xylan-degrading ability at 60°C on 0.5% xylan were further tested by using minimal medium with the addition of 0.1% RBB-xylan as a substrate. The results showed that these isolates were also able to utilized RBB-xylan at 45 to 60°C. The xylanolytic activity of the crude enzymes from the three isolates on minimal medium containing 0.5% xylan or 0.1% RBB-xylan as substrates, indicated that these isolates were able to produce extracellular xylanase. This study revealed that the soil of Cisolok geysers served as an ideal source for finding the thermophilic Actinobacteria which produced xylanase at high temperatures.

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Section: Phylogenetic Tree Analysessupporting

confidence: 58%

Xylan-degrading ability of thermophilic Actinobacteria from soil in a geothermal area

Rachmania¹,

Ningsih²,

Setyaningsih³

et al. 2019

Biodiversitas

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“…Protease C2 [106] showed a surprisingly high activity (24000%) on azocoll compared to keratin azure (100%). KERDZ [94], from the S1 peptidase family, had no activity on collagen, whereas RecGEOker [109], belonging to the M4 metallopeptidase family, was able to hydrolyse collagen. The differences in activity between substrates may be attributed to the specific peptide sequences in the substrates and the sequence specificity of the enzymes.…”

Section: Substrate Specificitymentioning

confidence: 99%

“…The S8 family has a minimum of 13.69% and a maximum of 99.72% identity, with an average of 63.29% for the 13 available sequences, and the M4 family has 25.56% identity between the two available sequences. Although many of the characterized enzymes have been produced by the native unmodified organism [94][95][96][97][98], several examples involve heterologous expression. Different organisms have been used for recombinant production, including yeast such as Komagataella Pastoris (Pichia Pastoris) [99] and bacteria such as Escherichia coli [100][101][102][103][104][105][106][107][108][109][110] and Streptomyces lividans [111].…”

Section: Characterisation and Comparison Of Keratinases From S1 S8 Amentioning

confidence: 99%

“…Except for KerQ7 [104], all assays in Table 4 were carried under alkaline conditions between pH 8 and pH 12.5 and temperatures ranging from 50 to 80 • C. These conditions would most likely contribute to the weakening the keratin structure. Keratinase assays with SAPDZ [100], KerQ7 [104], KERDZ [94], and KERAK-29 [95] were supplemented with the divalent cations Ca 2+ or Mn2 + . Divalent cations are known to stabilize serine proteases [114,117].…”

Section: Problems Associated With Keratinase Assaysmentioning

confidence: 99%

“…The two S8 family peptidases-SAPDZ [100] and KerRP [96]-appear to have similar ester substrate affinity with both showing activity against N-benzoyl-L-tyrosine ethyl ester (BTEE) and N-acetyl-L-tyrosine ethyl ester (ATEE). In contrast, KERDZ (S1 family) had no activity towards these substrates but was active towards N-α-benzoyl-L-arginine ethyl ester (BAEE), N-α-p-tosyl-L-arginine methyl (TAME) and benzoyl-citrulline ethyl ester (BCEE) [94].…”

Section: M4 Peptidasesmentioning

confidence: 99%

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

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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A Taguchi design approach for the enhancement of a detergent‐biocompatible alkaline thermostable protease production by Streptomyces mutabilis strain TN‐X30

Mechri

Bouacem

Chalbi

et al. 2022

J Surfact & Detergents

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The ability of microorganisms to grow at high temperature, alkaline pH, and high salinity makes them an attractive target for enzyme-production with several industrial applications. One strain TN-X30 has been selected as protease producer and identified as Streptomyces mutabilis after a phenotypic and molecular study. Its production of protease was improved using Taguchi L27 design. The strategy was carried out to identify the optimum levels and the interaction of the screened factors. Following this step, maximum protease activity (10,895 U/ml) was achieved after 6-days of incubation. The TN-X30 protease activity had an optimum of pH and temperature of 10 and 65 C, respectively. Thermodynamic parameters at 60 C were enthalpy 14.26 kJ/mol, entropy À220 J/mol/K, and Gibbs free energy 90.53 kJ/mol. TN-X30 protease production displayed a 16-fold increase reaching 175,000 U/ml in a 100-L fermentor. Furthermore, the lyophilization in presence of sorbitol enhanced the stability of the TN-X30 protease which remained active at 75% after 24-months of storage. The lyophilized TN-X30 protease exhibited exceptional stability indexes in presence of some known commercialized detergent components as NEODOL ® 25-7, Dehydol ® LT 7, Na 2 CMC, Galaxy LAS, Galaxy LES 70, Galaxy 110, Galaxy CAPB Plus, and Sulfacid K. The lyophilized enzyme also displayed high stability with respect to both solid and liquid detergents. Finally, TN-X30 protease exhibited remarkable destaining of blood, egg, and chocolate stained cloth pieces. These findings may promote TN-X30 protease for use as bioadditive in detergent formulation, thereby reducing environmental chemical threat.

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Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50

Cited by 43 publications

References 74 publications

Xylan-degrading ability of thermophilic Actinobacteria from soil in a geothermal area

Xylan-degrading ability of thermophilic Actinobacteria from soil in a geothermal area

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

A Taguchi design approach for the enhancement of a detergent‐biocompatible alkaline thermostable protease production by Streptomyces mutabilis strain TN‐X30

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