Heterologous expression and purification of keratinase from Actinomadura viridilutea DZ50: feather biodegradation and animal hide dehairing bioprocesses.
Animal hide dehairing
Feather degradation
Heterologous expression
Keratinase
Leather industry
Journal
Environmental science and pollution research international
ISSN: 1614-7499
Titre abrégé: Environ Sci Pollut Res Int
Pays: Germany
ID NLM: 9441769
Informations de publication
Date de publication:
Feb 2021
Feb 2021
Historique:
received:
02
04
2020
accepted:
21
10
2020
pubmed:
8
11
2020
medline:
20
2
2021
entrez:
7
11
2020
Statut:
ppublish
Résumé
The keratin-degrading bacterium Actinomadura viridilutea DZ50 secretes a keratinase (KERDZ) with potential industrial interest. Here, the kerDZ gene was extracellularly expressed in Escherichia coli BL21(DE3)pLysS using pTrc99A vector. The recombinant enzyme (rKERDZ) was purified and biochemically characterized. Results showed that the native and recombinant keratinases have similar biochemical characteristics. The conventional dehairing with lime and sodium sulfide degrades the hair to the extent that it cannot be recovered. Thus, these chemical processes become a major contributor to wastewater problem and create a lot of environmental concern. The complete dehairing was achieved with 2000 U/mL rKERDZ for 10 h at 40 °C. In fact, keratinase assisted dehairing entirely degraded chicken feather (45 mg) and removed wool/hair from rabbit, sheep, goat, or bovine' hides (1.6 kg) while preserving the collagen structure. The enzymatic process is the eco-friendly option that reduces biological (BOD) (50%) and chemical (COD) oxygen demands (60%) in leather processing. Consequently, the enzymatic hair removal process could solve the problem of post-treatments encountering the traditional leather processing. The enzymatic (rKERDZ) dehaired leather was analyzed by scanning electron microscopic (SEM) studies, which revealed similar fiber orientation and compactness compared with control sample. Those properties support that the rKERDZ enzyme-mediated process is greener to some extent than the traditional one.
Identifiants
pubmed: 33159682
doi: 10.1007/s11356-020-11371-1
pii: 10.1007/s11356-020-11371-1
doi:
Substances chimiques
Peptide Hydrolases
EC 3.4.-
keratinase
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
9921-9934Références
Abraham J, Gea T, Sánchez A (2014) Substitution of chemical dehairing by proteases from solid-state fermentation of hair wastes. J Clean Prod 74:191–198
doi: 10.1016/j.jclepro.2014.03.035
Asgher M, Bashir F, Iqbal HM (2018) Protease-based cross-linked enzyme aggregates with improved catalytic stability, silver removal, and dehairing potentials. Int J Biol Macromol 118:1247–1256
doi: 10.1016/j.ijbiomac.2018.06.107
Ben Elhoul M, Zaraî Jaouadi N, Rekik H, Benmrad Omrane M, Mechri S, Moujehed E, Kourdali S, El Hattab M, Badis A, Bejar S (2016) Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50. Int J Biol Macromol 92:299–315
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
doi: 10.1016/0003-2697(76)90527-3
Catalán Campillo E, Komilis D, Sánchez Ferrer A (2018) A life cycle assessment on the dehairing of rawhides: chemical treatment versus enzymatic recovery through solid state fermentation. J Ind Ecol 23:361–373
doi: 10.1111/jiec.12753
Dayanandan A, Sra J (2016) Determinants of earnings management in India: 2002-2011. Int J Account Financ 6:235–254
doi: 10.1504/IJAF.2016.081703
Gurav R, Nalavade V, Aware C, Vyavahare G, Bhatia SK, Yang YH, Bapat V, Jadhav J (2020) Microbial degradation of poultry feather biomass in a constructed bioreactor and application of hydrolysate as bioenhancer to vegetable crops. Environ Sci Pollut Res 27:2027–2035
doi: 10.1007/s11356-019-06536-6
Habbeche A, Saoudi B, Jaouadi B, Haberra S, Kerouaz B, Boudelaa M, Badis A, Ladjama A (2014) Purification and biochemical characterization of a detergent-stable keratinase from a newly thermophilic actinomycete Actinomadura keratinilytica strain Cpt29 isolated from poultry compost. J Biosci Bioeng 117:413–421
doi: 10.1016/j.jbiosc.2013.09.006
Hammami A, Fakhfakh N, Abdelhedi O, Nasri M, Bayoudh A (2018) Proteolytic and amylolytic enzymes from a newly isolated Bacillus mojavensis SA: characterization and applications as laundry detergent additive and in leather processing. Int J Biol Macromol 108:56–68
doi: 10.1016/j.ijbiomac.2017.11.148
He Z, Sun R, Tang Z, Bu T, Wu Q, Li C, Chen H (2018) Biodegradation of feather waste keratin by the keratin-degrading strain Bacillus subtilis 8. J Microbiol Biotechnol 28:314–322
doi: 10.4014/jmb.1708.08077
Jaouadi B, Aghajari N, Haser R, Bejar S (2010a) Enhancement of the thermostability and the catalytic efficiency of Bacillus pumilus CBS protease by site-directed mutagenesis. Biochimie 92:360–369
doi: 10.1016/j.biochi.2010.01.008
Jaouadi B, Abdelmalek B, Fodil D, Ferradji FZ, Rekik H, Zaraî N, Bejar S (2010b) Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents. Bioresour Technol 101:8361–8369
doi: 10.1016/j.biortech.2010.05.066
Kalaikumari SS, Vennila T, Monika V, Chandraraj K, Gunasekaran P, Rajendhran J (2019) Bioutilization of poultry feather for keratinase production and its application in leather industry. J Clean Prod 208:44–53
doi: 10.1016/j.jclepro.2018.10.076
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
doi: 10.1038/227680a0
Mechri S, Bouacem K, Zaraî Jaouadi N, Rekik H, Ben Elhoul M, Omrane Benmrad M, Hacene H, Bejar S, Bouanane-Darenfed A, Jaouadi B (2019) Identification of a novel protease from the thermophilic Anoxybacillus kamchatkensis M1V and its application as laundry detergent additive. Extremophiles 23:687–706
Reddy MR, Reddy KS, Chouhan YR, Bee H, Reddy G (2017) Effective feather degradation and keratinase production by Bacillus pumilus GRK for its application as bio-detergent additive. Bioresour Technol 243:254–263
doi: 10.1016/j.biortech.2017.06.067
Rieger T, De Oliveira C, Pereira J, Brandelli A, Daroit D (2017) Proteolytic system of Bacillus sp. CL18 is capable of extensive feather degradation and hydrolysis of diverse protein substrates. Bri Poul Sci 58:329–335
doi: 10.1080/00071668.2017.1293229
Shakilanishi S, Babu NKC, Shanthi C (2017) Exploration of chrome shaving hydrolysate as substrate for production of dehairing protease by Bacillus cereus VITSN04 for use in cleaner leather production. J Clean Prod 149:797–804
doi: 10.1016/j.jclepro.2017.02.139
Shin HD, Chen RR (2008) Extracellular recombinant protein production from an Escherichia coli lpp deletion mutant. Biotechnol Bioeng 101:1288–1296
doi: 10.1002/bit.22013
Sobucki L, Ramos RF, Daroit DJ (2017) Protease production by the keratinolytic Bacillus sp. CL18 through feather bioprocessing. Environ Sci Pollut Res 24:23125–23132
doi: 10.1007/s11356-017-9876-6
Sujitha P, Kavitha S, Shakilanishi S, Babu NKC, Shanthi C (2018) Enzymatic dehairing: a comprehensive review on the mechanistic aspects with emphasis on enzyme specificity. Int J Biol Macromol 118:168–179
doi: 10.1016/j.ijbiomac.2018.06.081
Tamreihao K, Mukherjee S, Khunjamayum R, Devi LJ, Asem RS, Ningthoujam DS (2018) Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production. J Basic Microbiol 59:4–13
doi: 10.1002/jobm.201800434
Tiwary E, Gupta R (2010) Extracellular expression of keratinase from Bacillus licheniformis ER-15 in Escherichia coli. J Agric Food Chem 58:8380–8385
doi: 10.1021/jf100803g
Ursula R, Elena GF, José LC, Esther V, Joaquin SF, Antonio V (2017) Bacterial inclusion bodies. Discovering their better half. Trends Biochem Sci 42:726–737
doi: 10.1016/j.tibs.2017.01.005
Valeika V, Širvaitytė J, Bridžiuvienė D, Švedienė J (2019) An application of advanced hair-save processes in leather industry as the reason of formation of keratinous waste: few peculiarities of its utilisation. Environ Sci Pollut Res 26:6223–6233
doi: 10.1007/s11356-019-04142-0
Xie F, Chao Y, Yang X, Yang J, Xue Z, Luo Y, Qian S (2010) Purification and characterization of four keratinases produced by Streptomyces sp. strain 16 in native human foot skin medium. Bioresour Technol 101:344–350
doi: 10.1016/j.biortech.2009.08.026
Yin J, Li G, Ren X, Herrler G (2007) Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. J Biotechnol 127:335–347
doi: 10.1016/j.jbiotec.2006.07.012
Zaraî Jaouadi N, Jaouadi B, Aghajari N, Bejar S (2012) The overexpression of the SAPB of Bacillus pumilus CBS and mutated sapB-L31I/T33S/N99Y alkaline proteases in Bacillus subtilis DB430: new attractive properties for the mutant enzyme. Bioresour Technol 105:142–151
Zaraî Jaouadi N, Rekik H, Badis A, Trabelsi S, Belhoul M, Yahiaoui Benkiar A, Ben Aicha H, Toumi A, Bejar S, Jaouadi B (2013) Biochemical and molecular characterization of a serine keratinase from Brevibacillus brevis US575 with promising keratin-biodegradation and hide-dehairing activities. PLoS One 8:e76722
Zaraî Jaouadi N, Jaouadi B, Ben Hlima H, Rekik H, Belhoul M, Hmidi M, Slimene Ben Aicha H, Hila Gorgi C, Toumi A, Aghajari N (2014) Probing the crucial role of Leu31 and Thr33 of the Bacillus pumilus CBS alkaline protease in substrate recognition and enzymatic depilation of animal hide. PLoS One 9:e108367
doi: 10.1371/journal.pone.0108367
Zaraî Jaouadi N, Rekik H, Ben Elhoul M, Rahem FZ, Hila Gorgi C, Slimene Ben Aicha H, Badis A, Toumi A, Bejar S, Jaouadi B (2015) A novel keratinase from Bacillus tequilensis strain Q7 with promising potential for the leather bating process. Int J Biol Macromol 79:952–964
doi: 10.1016/j.ijbiomac.2015.05.038
Zhou C, Qin H, Chen X, Zhang Y, Xue Y, Ma Y (2018) A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry. Sci Rep 8:16467
doi: 10.1038/s41598-018-34416-5