Keratinolytic Protease Production by Bacillus amyloliquefaciens 6B Using Feather Meal as Substrate and Application of Feather Hydrolysate as Organic Nitrogen Input for Agricultural Soil
Feather waste, a by-product of poultry processing sectors, contains a large quantity of hard to degrade keratin that pose great threat to the environment and mankind. Thus, development of a biotechnological approach to use such waste as substrate for enzyme production with its subsequent conversion...
Saved in:
Published in: | Waste and biomass valorization Vol. 5; no. 4; pp. 595 - 605 |
---|---|
Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
Dordrecht
Springer Netherlands
01-08-2014
|
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Abstract | Feather waste, a by-product of poultry processing sectors, contains a large quantity of hard to degrade
keratin
that pose great threat to the environment and mankind. Thus, development of a biotechnological approach to use such waste as substrate for enzyme production with its subsequent conversion to nitrogenous soil input is the main aim of the present investigation. Thirteen proteolytic bacteria were isolated from feather dump soil, amongst which
Bacillus amyloliquefaciens
6B (JQ904625) was found to completely degrade native feather in shortest time period (24 h) and thus selected for further investigation. Upon optimization of process parameters, the maximum enzyme yield (610.13 U/ml) was obtained after 12 h of fermentation at 37 °C using a medium containing 0.5 % (w/v) feather meal and 0.5 % (w/v) xylose at pH 8.0. The keratinolytic protease 6B exhibited optimum activity at 50 °C and pH 8.0. The enzyme exhibited significant stability in presence of solvents, surfactants and bleach-oxidant, suggesting its potential use in industries. Furthermore, the strain could produce antifungal metabolites which could inhibit the growth of fungal phytopathogens in the same conditions observed for keratinolytic enzyme production. Consequently, feather hydrolysates resulting from the microbial conversion of feather keratin might be utilized as a bioactive agricultural nitrogen input. Thus, degradation of bird feather using a soil bacterial isolate with simultaneous production of solvent and detergent tolerant keratinolytic protease, offers a cost-effective technology for industrial protease production, while adding value to poultry feather waste. |
---|---|
AbstractList | Feather waste, a by-product of poultry processing sectors, contains a large quantity of hard to degrade
keratin
that pose great threat to the environment and mankind. Thus, development of a biotechnological approach to use such waste as substrate for enzyme production with its subsequent conversion to nitrogenous soil input is the main aim of the present investigation. Thirteen proteolytic bacteria were isolated from feather dump soil, amongst which
Bacillus amyloliquefaciens
6B (JQ904625) was found to completely degrade native feather in shortest time period (24 h) and thus selected for further investigation. Upon optimization of process parameters, the maximum enzyme yield (610.13 U/ml) was obtained after 12 h of fermentation at 37 °C using a medium containing 0.5 % (w/v) feather meal and 0.5 % (w/v) xylose at pH 8.0. The keratinolytic protease 6B exhibited optimum activity at 50 °C and pH 8.0. The enzyme exhibited significant stability in presence of solvents, surfactants and bleach-oxidant, suggesting its potential use in industries. Furthermore, the strain could produce antifungal metabolites which could inhibit the growth of fungal phytopathogens in the same conditions observed for keratinolytic enzyme production. Consequently, feather hydrolysates resulting from the microbial conversion of feather keratin might be utilized as a bioactive agricultural nitrogen input. Thus, degradation of bird feather using a soil bacterial isolate with simultaneous production of solvent and detergent tolerant keratinolytic protease, offers a cost-effective technology for industrial protease production, while adding value to poultry feather waste. |
Author | Keharia, Haresh Pathan, Shabnam Bose, Anjali Pathak, Khyati |
Author_xml | – sequence: 1 givenname: Anjali surname: Bose fullname: Bose, Anjali organization: BRD School of Biosciences, Sardar Patel Maidan, Satellite Campus, Sardar Patel University – sequence: 2 givenname: Shabnam surname: Pathan fullname: Pathan, Shabnam organization: BRD School of Biosciences, Sardar Patel Maidan, Satellite Campus, Sardar Patel University – sequence: 3 givenname: Khyati surname: Pathak fullname: Pathak, Khyati organization: BRD School of Biosciences, Sardar Patel Maidan, Satellite Campus, Sardar Patel University – sequence: 4 givenname: Haresh surname: Keharia fullname: Keharia, Haresh email: haresh970@gmail.com organization: BRD School of Biosciences, Sardar Patel Maidan, Satellite Campus, Sardar Patel University |
BookMark | eNp9UEtOwzAUtFCRKJ8DsPMFAnacxPGyrShFfCVAYhc5jh1cuXaxnUWOxu1wKeqSxdN7Gs3MG80pmFhnJQCXGF1hhOh1wHlVsAxhkrGc5ll5BKa4pjTLq_JjcrgLfAIuQlgjhHKM65zQKfi-l55HbZ0ZoxbwxbsoeZC7oxtE1M7CdoRzLrQxQ4B8Mxpn9NcgVYKkDbCaw_egbQ-XksdP6eGj5AbyAF-HNsTkLSG3HZxtt0YL_mvo1IG8GjufXodfWoDPvuc2xXjS0bteWnhnt0OEynk4670Wg4mDT_avTptzcKy4CfLib5-B9-XN22KVPTzf3i1mD5nI6zpmtaw6wgRDqGWISkJU0SpMiWK0QKpjLCGsErgmVVdWpKRtUfO6RKTtMOFpzgDe-wrvQvBSNVuvN9yPDUbNrv5mX3-T6m929Tdl0uR7TUhc20vfrN3gbYr5j-gHodmNtA |
CitedBy_id | crossref_primary_10_1007_s40093_019_0281_7 crossref_primary_10_1080_00071668_2017_1278627 crossref_primary_10_1016_j_bcab_2017_04_004 crossref_primary_10_3390_molecules25071505 crossref_primary_10_3389_fbioe_2021_720176 crossref_primary_10_15407_biotech8_02_084 crossref_primary_10_1007_s12010_020_03355_1 crossref_primary_10_1007_s12649_016_9694_y crossref_primary_10_1016_j_envres_2023_115283 crossref_primary_10_1007_s11756_021_00724_x crossref_primary_10_1007_s12649_015_9464_2 crossref_primary_10_1080_10242422_2020_1746770 crossref_primary_10_1007_s12649_021_01556_1 crossref_primary_10_1007_s10123_018_0022_1 crossref_primary_10_1007_s12649_023_02123_6 crossref_primary_10_1007_s11270_023_06831_6 crossref_primary_10_1016_j_envres_2023_117907 crossref_primary_10_3389_fmicb_2022_918262 crossref_primary_10_3390_microorganisms8091304 crossref_primary_10_1007_s12649_016_9603_4 crossref_primary_10_1080_10242422_2017_1280031 crossref_primary_10_1080_09593330_2022_2102938 crossref_primary_10_1016_j_eti_2020_101285 crossref_primary_10_1016_j_bcab_2015_07_002 crossref_primary_10_1007_s11356_017_9876_6 crossref_primary_10_1016_j_bcab_2021_102174 crossref_primary_10_1016_j_psj_2022_102027 crossref_primary_10_1007_s13399_022_03684_7 crossref_primary_10_1039_C7BM00411G crossref_primary_10_1007_s42398_021_00160_2 crossref_primary_10_1016_j_biochi_2020_08_005 crossref_primary_10_1007_s12649_021_01472_4 crossref_primary_10_1007_s12649_024_02532_1 crossref_primary_10_1007_s00253_020_10528_9 crossref_primary_10_1007_s00284_021_02491_z crossref_primary_10_29252_jhehp_2_1_39 crossref_primary_10_1016_j_bcab_2017_04_010 crossref_primary_10_1016_j_psep_2022_12_029 crossref_primary_10_1016_j_wasman_2019_06_040 crossref_primary_10_13005_bbra_3136 crossref_primary_10_1016_j_jwpe_2020_101707 crossref_primary_10_1080_00071668_2017_1293229 crossref_primary_10_1016_j_jclepro_2019_119847 crossref_primary_10_1016_j_ijbiomac_2018_03_046 crossref_primary_10_3389_fmicb_2020_580164 |
Cites_doi | 10.1128/AEM.58.10.3271-3275.1992 10.1016/j.procbio.2011.05.023 10.1007/s00203-002-0489-0 10.1016/j.ibiod.2009.12.007 10.1016/j.anifeedsci.2005.06.002 10.1007/s00792-005-0491-y 10.1128/MMBR.59.2.201-222.1995 10.1016/0922-338X(91)90109-T 10.1016/j.ibiod.2010.04.014 10.1007/s00203-003-0525-8 10.1271/bbb.56.246 10.1128/AEM.68.12.6210-6219.2002 10.1007/s11947-007-0025-y 10.1016/j.ibiod.2009.07.003 10.1016/0300-9084(92)90002-V 10.1016/S0141-0229(03)00004-8 10.1016/j.jhazmat.2005.02.003 10.1016/j.wasman.2008.10.009 10.1016/S0960-8524(98)00033-9 10.1023/A:1020501420831 10.1016/j.micres.2007.02.004 10.1042/BA20030228 10.1002/1097-0231(20010215)15:3<203::AID-RCM212>3.0.CO;2-6 10.1002/(SICI)1097-0231(19990530)13:10<880::AID-RCM574>3.0.CO;2-1 10.1007/s11274-008-9782-7 10.1002/(SICI)1097-0010(199702)73:2<242::AID-JSFA712>3.0.CO;2-3 10.1023/A:1007086720237 10.1007/s10295-009-0565-4 10.1016/j.enzmictec.2005.02.021 10.1007/978-1-4613-0319-0_12 10.1016/j.molcatb.2008.08.001 10.1016/j.micres.2006.06.007 10.1002/bit.260300112 10.1016/j.bej.2008.10.001 10.1006/jmbi.1999.3291 10.1271/bbb.59.2239 10.1016/j.procbio.2010.07.020 10.1038/227680a0 10.1016/j.tim.2007.12.009 10.1016/j.biortech.2009.08.026 10.3923/jbs.2007.599.606 10.1016/j.biotechadv.2011.04.002 10.1007/s12010-009-8702-0 10.1007/s00253-005-0239-8 10.1007/s00253-008-1429-y 10.1631/jzus.B061620 10.1046/j.1472-765X.2002.01093.x 10.1016/S0021-9258(19)52451-6 |
ContentType | Journal Article |
Copyright | Springer Science+Business Media Dordrecht 2013 |
Copyright_xml | – notice: Springer Science+Business Media Dordrecht 2013 |
DBID | AAYXX CITATION |
DOI | 10.1007/s12649-013-9272-5 |
DatabaseName | CrossRef |
DatabaseTitle | CrossRef |
DatabaseTitleList | |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering |
EISSN | 1877-265X |
EndPage | 605 |
ExternalDocumentID | 10_1007_s12649_013_9272_5 |
GroupedDBID | -EM 06D 0R~ 0VY 1N0 203 29~ 2JY 2VQ 30V 4.4 406 408 409 40D 8TC 96X AAAVM AAFGU AAHNG AAIAL AAJKR AANZL AAPBV AARHV AARTL AATLR AATNV AATVU AAUYE AAWCG AAYFA AAYIU AAYQN AAYTO AAZMS ABBXA ABDZT ABECU ABFGW ABFTV ABHQN ABJNI ABJOX ABKAS ABKCH ABMQK ABQBU ABSXP ABTEG ABTHY ABTKH ABTMW ABULA ABWNU ABXPI ACBMV ACBRV ACBYP ACGFS ACHSB ACIGE ACIPQ ACKNC ACMLO ACOKC ACTTH ACVWB ACWMK ADHHG ADHIR ADINQ ADKNI ADKPE ADMDM ADOXG ADRFC ADTPH ADURQ ADYFF ADZKW AEBTG AEFTE AEGNC AEJHL AEJRE AENEX AEOHA AEPYU AESKC AESTI AETCA AEVLU AEVTX AEXYK AFLOW AFNRJ AFQWF AFRAH AFWTZ AFZKB AGAYW AGDGC AGGBP AGJBK AGMZJ AGQMX AGWZB AGYKE AHAVH AHBYD AHSBF AHYZX AIAKS AIIXL AILAN AIMYW AITGF AJBLW AJDOV AJRNO AJZVZ AKLTO AKQUC ALFXC ALMA_UNASSIGNED_HOLDINGS AMKLP AMXSW AMYLF AMYQR ANMIH ASPBG AUKKA AVWKF AXYYD AYJHY AZFZN BGNMA CSCUP DNIVK DPUIP EBLON EBS EIOEI EJD ESBYG FEDTE FERAY FFXSO FIGPU FINBP FNLPD FRRFC FSGXE FYJPI GGCAI GGRSB GJIRD GQ6 GQ7 GQ8 HF~ HG6 HMJXF HQYDN HRMNR HVGLF HZ~ I0C IKXTQ IWAJR IXD IZIGR J-C J0Z JBSCW JCJTX JZLTJ KOV LLZTM M4Y NPVJJ NQJWS NU0 O9- O93 O9J P2P P9P PT4 QOS R89 R9I RIG RLLFE ROL RSV S1Z S27 S3B SEG SHX SISQX SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW STPWE T13 TSG U2A UG4 UOJIU UTJUX UZXMN VFIZW W48 WK8 Z45 Z5O Z7R Z7U Z7V Z7W Z7X Z7Y Z7Z Z81 Z83 Z85 ZMTXR ~A9 AACDK AAHBH AAJBT AASML AAYXX AAYZH ABAKF ACAOD ACDTI ACZOJ AEFQL AEMSY AFBBN AGQEE AIGIU CITATION H13 SJYHP |
ID | FETCH-LOGICAL-c288t-8e6d39c900b907e33f4bf173f9740fd9933f96c1836d56357b48a8503bd13ad13 |
IEDL.DBID | AEJHL |
ISSN | 1877-2641 |
IngestDate | Thu Nov 21 22:09:31 EST 2024 Sat Dec 16 12:12:39 EST 2023 |
IsPeerReviewed | false |
IsScholarly | true |
Issue | 4 |
Keywords | Surfactin Feather degrading Nitrogenous soil input Solvent tolerant serine protease |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c288t-8e6d39c900b907e33f4bf173f9740fd9933f96c1836d56357b48a8503bd13ad13 |
PageCount | 11 |
ParticipantIDs | crossref_primary_10_1007_s12649_013_9272_5 springer_journals_10_1007_s12649_013_9272_5 |
PublicationCentury | 2000 |
PublicationDate | 2014-08-01 |
PublicationDateYYYYMMDD | 2014-08-01 |
PublicationDate_xml | – month: 08 year: 2014 text: 2014-08-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | Dordrecht |
PublicationPlace_xml | – name: Dordrecht |
PublicationTitle | Waste and biomass valorization |
PublicationTitleAbbrev | Waste Biomass Valor |
PublicationYear | 2014 |
Publisher | Springer Netherlands |
Publisher_xml | – name: Springer Netherlands |
References | SambrookJRussellDWMolecular Cloning: A Laboratory Manual2001New YorkCold Spring Harbor Laboratory Press TrivediPPandyAPalniLMIn vitro evaluation of antagonistic properties of Pseudomonas corrugataMicrobiol. Res.200816332933610.1016/j.micres.2006.06.007 Maget-DanaRThimonLPeypouxFPtakMSurfactin/iturin A interactions may explain the synergistic effect of surfactin on the biological properties of iturin ABiochimie1992741047105110.1016/0300-9084(92)90002-V CaiCGZhengXDMedium optimization for keratinase production in hair substrate by a new Bacillus subtilis KD-N2 using response surface methodologyJ. Ind. Microbiol. Biotechnol.20093687588310.1007/s10295-009-0565-4 NamGWLeeDWLeeHSLeeNJKimBCChoeEAHwangJKSuhartonoMTPyunYRNative-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobeArch. Microbiol.200217853854710.1007/s00203-002-0489-0 Pathak, K.V.: Purification and Characterization of Antifungal Compounds Produced by Banyan Endophytic Bacilli. Ph.D. Thesis, Sardar Patel University, Vallabh Vidyanagar, India. (2011) GrazziotinAPimentelFAde JongEVBrandelliANutritional improvement of feather protein by treatment with microbial keratinaseAnim. Feed Sci. Technol.200612613514410.1016/j.anifeedsci.2005.06.002 TorresSPandeyACastroGROrganic solvent adaptation of gram positive bacteria: applications and biotechnological potentialsBiotechnol. Adv.20112944245210.1016/j.biotechadv.2011.04.002 DeydierEGuiletRSardaSSharrockPPhysical and chemical characterization of crude meat and bone meal combustion residue: waste or raw material?J. Hazard. Mater.200512114114810.1016/j.jhazmat.2005.02.003 LiSHeBBaiZOuyangPA novel organic solvent-stable alkaline protease from organic solvent-tolerant Bacillus licheniformis YP1AJ. Mol. Catal. B200956858810.1016/j.molcatb.2008.08.001 FangYLiuSWangSLvMIsolation and screening of a novel extracellular organic solvent-stable protease producerBiochem. Eng. J.20094321221510.1016/j.bej.2008.10.001 Vasileva-TonkovaEGousterovaANeshevGEcologically safe method for improved feather wastes biodegradationInt. Biodeterior. Biodegradation2009631008101210.1016/j.ibiod.2009.07.003 SikkemaJde BontJAMPoolmanBMechanisms of membrane toxicity of hydrocarbonsMicrobiol. Rev.199559201222 GuptaRRamnaniPMicrobial keratinase and their prospective application: an overviewAppl. Microbiol. Biotechnol.200670213310.1007/s00253-005-0239-8 BernalCCairoJCoelloNPurification and characterization of a novel exocellular keratinase from Kocuria roseaEnzym. Microb. Technol.200638495410.1016/j.enzmictec.2005.02.021 LateefAOlokeJKGueguim KanaEBSobowaleBOAjaoSOBelloBYKeratinolytic activities of a new feather-degrading isolate of Bacillus cereus LAU 08 isolated from Nigerian soilInt. Biodeterior. Biodegradation20106416216510.1016/j.ibiod.2009.12.007 LaemmliUKCleavage of structural proteins during the assembly of the head of bacteriophage T4Nature197022768068510.1038/227680a0 RaaijmakersJMVlamiMSouzaJTAntibiotic production by bacterial biocontrol agentsAntonie Van Leeuwenhoek20028153754710.1023/A:1020501420831 BrandelliABacterial keratinases: useful enzymes for bioprocessing agroindustrial wastes and beyondFood Bioprocess Technol.2008110511610.1007/s11947-007-0025-y ChengSWHuHMShenSWTakagiHAsanoMTsaiYCProduction and characterization of keratinase of a feather-degrading Bacillus licheniformis PWD-1Biosci. Biotechnol. Biochem.1995592239224310.1271/bbb.59.2239 HueNSeraniLLaprevoteOStructural investigation of cyclic peptidolipids from Bacillus subtilis by high energy tandem mass spectrometryRapid Commun. Mass Spectrom.20011520320910.1002/1097-0231(20010215)15:3<203::AID-RCM212>3.0.CO;2-6 FAO. http://www.fao.org/docrep/004/AD452E/ad452e30.htm (2002) VaterJKablitzBWildeCFrankePMehtaNCameotraSSMatrix-assisted laser desorption ionization-time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludgeAppl. Environ. Microbiol.2002686210621910.1128/AEM.68.12.6210-6219.2002 KojimaMKanaiMTominagaMKitazumeSInoueAHorikoshiKIsolation and characterization of a feather degrading enzyme from Bacillus pseudofirmus FA30-01Extremophiles20061022923510.1007/s00792-005-0491-y GhorbelBSellami-KamounANasriMStability studies of protease from Bacillus cereus BG1Enzym. Microb. Technol.20033251351810.1016/S0141-0229(03)00004-8 DalevPIvanovILiubomirovaAEnzymic modification of feather keratin hydrolyzates with lysine aimed at increasing the biological valueJ. Sci. Food Agric.19977324224410.1002/(SICI)1097-0010(199702)73:2<242::AID-JSFA712>3.0.CO;2-3 PrakashPJayalakshmiSKSreeramuluKProduction of keratinases by free and immobilized cells of Bacillus halodurans strain PPKS-2: partial characterization and its application in feather degradation and dehairing of the goat skinAppl. Biochem. Biotechnol.20101601909192010.1007/s12010-009-8702-0 SmithCAToogoodHSBakerHMDanielRMBakerENCalcium-mediated thermostability in the Subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 Å resolutionJ. Mol. Biol.19992941027104010.1006/jmbi.1999.3291 XieFChaoYYangXYangJXueZLuoYQianSPurification and characterization of four keratinases produced by Streptomyces sp. strain 16 in native human foot skin mediumBioresour. Technol.201010134435010.1016/j.biortech.2009.08.026 CavelierFEnjalbalJMRoqueMSanchezPAubagnacJ-LComparison of collisionally dissociation mass spectra for the identification of cyclopeptides and cyclodepsipeptidesRapid Commun. Mass Spectrom.19991388088510.1002/(SICI)1097-0231(19990530)13:10<880::AID-RCM574>3.0.CO;2-1 LowryOHRosebroughNJFarrALRandallRJProtein measurement with the Folin phenol reagentJ. Biol. Chem.1951193265275 SareenRMishraPPurification and characterization of organic solvent stable protease from Bacillus licheniformis RSP-09-37Appl. Microbiol. Biotechnol.20087939940510.1007/s00253-008-1429-y KunertJKushwahaRKSGuarroJPhysiology of keratinophylic fungiBiology of Dermatophytes and Other Keratinophylic Fungi2000BilbaoRevista Iberoamericana de Micología7785 JeongJ-HLeeO-MJeonY-DKimJ-DLeeN-RLeeC-YSonH-JProduction of keratinolytic enzyme by a newly isolated feather-degrading Stenotrophomonas maltophilia that produces plant growth-promoting activityProcess Biochem.2010451738174510.1016/j.procbio.2010.07.020 KhardenavisAAKapleyAPurohitHJProcessing of poultry feathers by alkaline keratin hydrolyzing enzyme from Serratia sp. HPC 1383Waste Manag.2009291409141510.1016/j.wasman.2008.10.009 RiffelALucasFSHeebPBrandelliACharacterization of a new keratinolytic bacterium that completely degrades native feather keratinArch. Microbiol.2003179258265 LaaneCBoerenSVosKVeegerCRules for optimization of biocatalysis in organic solventsBiotechnol. Bioeng.198730818710.1002/bit.260300112 CaiCGLouBGZhengXDPurification and characterization of keratinase from a new Bacillus subtilis strainJ. Zhejiang Univ. Sci. B20089606710.1631/jzus.B061620 ParkGTSonHJKeratinolytic activity of Bacillus megaterium F7-1, a feather degrading mesophilic bacteriumMicrobiol. Res.200916447848510.1016/j.micres.2007.02.004 FakhfakhNKtariNHaddarAMnifIHDahmenINasriMTotal solubilisation of the chicken feathers by fermentation with a keratinolytic bacterium, Bacillus pumilus A1, and the production of protein hydrolysate with high antioxidative activityProcess Biochem.2011461731173710.1016/j.procbio.2011.05.023 BalajiSSenthil KumarMKarthikeyanRKumarRKirubanandanSSridharRSehgalPKPurification and characterization of an extracellular keratinase from a hornmeal-degrading Bacillus subtilis MTCC 9102World J. Microbiol. Biotechnol.2008242741274510.1007/s11274-008-9782-7 LinXLeeCGCasaleESShihJCHPurification and characterization of a keratinase from a feather degrading Bacillus licheniformis strainAppl. Environ. Microbiol.19925832713275 OnifadeAAAl-SaneNAAl-MusallamAAAl-ZarbanSA review: potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resourcesBioresour. Technol.19986611110.1016/S0960-8524(98)00033-9 OngenaMJacquesPBacillus lipopeptides: versatile weapons for plant disease biocontrolTrends Microbiol.20081611512510.1016/j.tim.2007.12.009 KimJMChoiYMSuhHJPreparation of feather digests as fertilizer with B. pumilus KHS-1J. Microbiol. Biotechnol.200515472476 HossainMSAzadAKAbu SayemSMMostafaGHoqMMProduction and partial characterization of feather-degrading keratinolytic serine protease from Bacillus licheniformis MZK-3J. Biol. Sci.2007759960610.3923/jbs.2007.599.606 WolffAMShowellMSVenegasMGBarnettBLWertzWCBottRBetzelCLaundry performance of subtilisin proteasesSubtilisin Enzymes: Practical Protein Engineering1996New YorkPlenum Press11312010.1007/978-1-4613-0319-0_12 TuschiyaKNakamuraYSakashitaHKimuraTPurification and characterization of a thermostable alkaline protease from alkalophilic Thermoactinomyces sp. HS682Biosci. Biotechnol. Biochem.19925624625010.1271/bbb.56.246 DaroitDJCorrêaAPFBrandelliAProduction of keratinolytic proteases through bioconversion of feather meal by the Amazonian bacterium Bacillus sp. P45Int. Biodeterior. Biodegradation201165455110.1016/j.ibiod.2010.04.014 InoueAHorikoshiKEstimation of solvent-tolerance of bacteria by the solvent parameter logPJ. Ferment. Bioeng.19917119419610.1016/0922-338X(91)90109-T KaulSSumbaliGProduction of extracellular keratinases by keratinolytic fungal species inhabiting feathers of living poultry birds (Gallus domesticus): a comparisonMycopathologia1999146192410.1023/A:1007086720237 RamnaniPGuptaGOptimization of medium composition for keratinase production on feather by Bacillus licheniformis RG1 using statistical methods involving response surface methodologyBiotechnol. Appl. Biochem.20044019119610.1042/BA20030228 AllpressJDMountainGGowlandPCProduction, purification and characterization of an extracellular keratinase from Lysobacter NCIMB 9497Lett. Appl. Microbiol.20023433734210.1046/j.1472-765X.2002.01093.x E Vasileva-Tonkova (9272_CR9) 2009; 63 S Torres (9272_CR25) 2011; 29 F Cavelier (9272_CR49) 1999; 13 R Gupta (9272_CR8) 2006; 70 CA Smith (9272_CR44) 1999; 294 X Lin (9272_CR38) 1992; 58 R Sareen (9272_CR22) 2008; 79 OH Lowry (9272_CR17) 1951; 193 M Ongena (9272_CR47) 2008; 16 F Xie (9272_CR43) 2010; 101 K Tuschiya (9272_CR45) 1992; 56 J Vater (9272_CR48) 2002; 68 P Trivedi (9272_CR15) 2008; 163 GT Park (9272_CR30) 2009; 164 C Bernal (9272_CR27) 2006; 38 S Kaul (9272_CR34) 1999; 146 R Maget-Dana (9272_CR52) 1992; 74 9272_CR51 A Inoue (9272_CR19) 1991; 71 JD Allpress (9272_CR41) 2002; 34 A Brandelli (9272_CR5) 2008; 1 SW Cheng (9272_CR36) 1995; 59 S Li (9272_CR24) 2009; 56 M Kojima (9272_CR39) 2006; 10 J Kunert (9272_CR33) 2000 Y Fang (9272_CR23) 2009; 43 P Ramnani (9272_CR32) 2004; 40 J Sikkema (9272_CR20) 1995; 59 P Prakash (9272_CR42) 2010; 160 CG Cai (9272_CR26) 2008; 9 UK Laemmli (9272_CR13) 1970; 227 JM Raaijmakers (9272_CR10) 2002; 81 E Deydier (9272_CR2) 2005; 121 AA Onifade (9272_CR4) 1998; 66 DJ Daroit (9272_CR31) 2011; 65 J Sambrook (9272_CR14) 2001 N Hue (9272_CR50) 2001; 15 J-H Jeong (9272_CR6) 2010; 45 S Balaji (9272_CR40) 2008; 24 B Ghorbel (9272_CR21) 2003; 32 AM Wolff (9272_CR46) 1996 CG Cai (9272_CR35) 2009; 36 P Dalev (9272_CR3) 1997; 73 N Fakhfakh (9272_CR12) 2011; 46 MS Hossain (9272_CR37) 2007; 7 GW Nam (9272_CR28) 2002; 178 A Riffel (9272_CR29) 2003; 179 A Lateef (9272_CR7) 2010; 64 C Laane (9272_CR18) 1987; 30 JM Kim (9272_CR53) 2005; 15 9272_CR1 A Grazziotin (9272_CR11) 2006; 126 AA Khardenavis (9272_CR16) 2009; 29 |
References_xml | – volume: 58 start-page: 3271 year: 1992 ident: 9272_CR38 publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.58.10.3271-3275.1992 contributor: fullname: X Lin – volume: 46 start-page: 1731 year: 2011 ident: 9272_CR12 publication-title: Process Biochem. doi: 10.1016/j.procbio.2011.05.023 contributor: fullname: N Fakhfakh – volume: 178 start-page: 538 year: 2002 ident: 9272_CR28 publication-title: Arch. Microbiol. doi: 10.1007/s00203-002-0489-0 contributor: fullname: GW Nam – volume: 64 start-page: 162 year: 2010 ident: 9272_CR7 publication-title: Int. Biodeterior. Biodegradation doi: 10.1016/j.ibiod.2009.12.007 contributor: fullname: A Lateef – volume: 126 start-page: 135 year: 2006 ident: 9272_CR11 publication-title: Anim. Feed Sci. Technol. doi: 10.1016/j.anifeedsci.2005.06.002 contributor: fullname: A Grazziotin – volume: 10 start-page: 229 year: 2006 ident: 9272_CR39 publication-title: Extremophiles doi: 10.1007/s00792-005-0491-y contributor: fullname: M Kojima – volume: 59 start-page: 201 year: 1995 ident: 9272_CR20 publication-title: Microbiol. Rev. doi: 10.1128/MMBR.59.2.201-222.1995 contributor: fullname: J Sikkema – volume: 71 start-page: 194 year: 1991 ident: 9272_CR19 publication-title: J. Ferment. Bioeng. doi: 10.1016/0922-338X(91)90109-T contributor: fullname: A Inoue – volume: 65 start-page: 45 year: 2011 ident: 9272_CR31 publication-title: Int. Biodeterior. Biodegradation doi: 10.1016/j.ibiod.2010.04.014 contributor: fullname: DJ Daroit – volume: 179 start-page: 258 year: 2003 ident: 9272_CR29 publication-title: Arch. Microbiol. doi: 10.1007/s00203-003-0525-8 contributor: fullname: A Riffel – ident: 9272_CR51 – volume: 56 start-page: 246 year: 1992 ident: 9272_CR45 publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.56.246 contributor: fullname: K Tuschiya – volume: 68 start-page: 6210 year: 2002 ident: 9272_CR48 publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.68.12.6210-6219.2002 contributor: fullname: J Vater – volume: 1 start-page: 105 year: 2008 ident: 9272_CR5 publication-title: Food Bioprocess Technol. doi: 10.1007/s11947-007-0025-y contributor: fullname: A Brandelli – ident: 9272_CR1 – volume: 63 start-page: 1008 year: 2009 ident: 9272_CR9 publication-title: Int. Biodeterior. Biodegradation doi: 10.1016/j.ibiod.2009.07.003 contributor: fullname: E Vasileva-Tonkova – volume: 74 start-page: 1047 year: 1992 ident: 9272_CR52 publication-title: Biochimie doi: 10.1016/0300-9084(92)90002-V contributor: fullname: R Maget-Dana – volume: 32 start-page: 513 year: 2003 ident: 9272_CR21 publication-title: Enzym. Microb. Technol. doi: 10.1016/S0141-0229(03)00004-8 contributor: fullname: B Ghorbel – volume: 121 start-page: 141 year: 2005 ident: 9272_CR2 publication-title: J. Hazard. Mater. doi: 10.1016/j.jhazmat.2005.02.003 contributor: fullname: E Deydier – volume: 29 start-page: 1409 year: 2009 ident: 9272_CR16 publication-title: Waste Manag. doi: 10.1016/j.wasman.2008.10.009 contributor: fullname: AA Khardenavis – volume: 66 start-page: 1 year: 1998 ident: 9272_CR4 publication-title: Bioresour. Technol. doi: 10.1016/S0960-8524(98)00033-9 contributor: fullname: AA Onifade – volume: 81 start-page: 537 year: 2002 ident: 9272_CR10 publication-title: Antonie Van Leeuwenhoek doi: 10.1023/A:1020501420831 contributor: fullname: JM Raaijmakers – volume: 164 start-page: 478 year: 2009 ident: 9272_CR30 publication-title: Microbiol. Res. doi: 10.1016/j.micres.2007.02.004 contributor: fullname: GT Park – volume: 40 start-page: 191 year: 2004 ident: 9272_CR32 publication-title: Biotechnol. Appl. Biochem. doi: 10.1042/BA20030228 contributor: fullname: P Ramnani – volume: 15 start-page: 203 year: 2001 ident: 9272_CR50 publication-title: Rapid Commun. Mass Spectrom. doi: 10.1002/1097-0231(20010215)15:3<203::AID-RCM212>3.0.CO;2-6 contributor: fullname: N Hue – volume: 13 start-page: 880 year: 1999 ident: 9272_CR49 publication-title: Rapid Commun. Mass Spectrom. doi: 10.1002/(SICI)1097-0231(19990530)13:10<880::AID-RCM574>3.0.CO;2-1 contributor: fullname: F Cavelier – volume: 24 start-page: 2741 year: 2008 ident: 9272_CR40 publication-title: World J. Microbiol. Biotechnol. doi: 10.1007/s11274-008-9782-7 contributor: fullname: S Balaji – volume: 73 start-page: 242 year: 1997 ident: 9272_CR3 publication-title: J. Sci. Food Agric. doi: 10.1002/(SICI)1097-0010(199702)73:2<242::AID-JSFA712>3.0.CO;2-3 contributor: fullname: P Dalev – volume: 146 start-page: 19 year: 1999 ident: 9272_CR34 publication-title: Mycopathologia doi: 10.1023/A:1007086720237 contributor: fullname: S Kaul – volume: 36 start-page: 875 year: 2009 ident: 9272_CR35 publication-title: J. Ind. Microbiol. Biotechnol. doi: 10.1007/s10295-009-0565-4 contributor: fullname: CG Cai – volume: 38 start-page: 49 year: 2006 ident: 9272_CR27 publication-title: Enzym. Microb. Technol. doi: 10.1016/j.enzmictec.2005.02.021 contributor: fullname: C Bernal – start-page: 113 volume-title: Subtilisin Enzymes: Practical Protein Engineering year: 1996 ident: 9272_CR46 doi: 10.1007/978-1-4613-0319-0_12 contributor: fullname: AM Wolff – volume: 56 start-page: 85 year: 2009 ident: 9272_CR24 publication-title: J. Mol. Catal. B doi: 10.1016/j.molcatb.2008.08.001 contributor: fullname: S Li – start-page: 77 volume-title: Biology of Dermatophytes and Other Keratinophylic Fungi year: 2000 ident: 9272_CR33 contributor: fullname: J Kunert – volume: 163 start-page: 329 year: 2008 ident: 9272_CR15 publication-title: Microbiol. Res. doi: 10.1016/j.micres.2006.06.007 contributor: fullname: P Trivedi – volume: 30 start-page: 81 year: 1987 ident: 9272_CR18 publication-title: Biotechnol. Bioeng. doi: 10.1002/bit.260300112 contributor: fullname: C Laane – volume: 43 start-page: 212 year: 2009 ident: 9272_CR23 publication-title: Biochem. Eng. J. doi: 10.1016/j.bej.2008.10.001 contributor: fullname: Y Fang – volume: 294 start-page: 1027 year: 1999 ident: 9272_CR44 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.3291 contributor: fullname: CA Smith – volume: 59 start-page: 2239 year: 1995 ident: 9272_CR36 publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.59.2239 contributor: fullname: SW Cheng – volume: 45 start-page: 1738 year: 2010 ident: 9272_CR6 publication-title: Process Biochem. doi: 10.1016/j.procbio.2010.07.020 contributor: fullname: J-H Jeong – volume: 15 start-page: 472 year: 2005 ident: 9272_CR53 publication-title: J. Microbiol. Biotechnol. contributor: fullname: JM Kim – volume: 227 start-page: 680 year: 1970 ident: 9272_CR13 publication-title: Nature doi: 10.1038/227680a0 contributor: fullname: UK Laemmli – volume: 16 start-page: 115 year: 2008 ident: 9272_CR47 publication-title: Trends Microbiol. doi: 10.1016/j.tim.2007.12.009 contributor: fullname: M Ongena – volume: 101 start-page: 344 year: 2010 ident: 9272_CR43 publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2009.08.026 contributor: fullname: F Xie – volume: 7 start-page: 599 year: 2007 ident: 9272_CR37 publication-title: J. Biol. Sci. doi: 10.3923/jbs.2007.599.606 contributor: fullname: MS Hossain – volume: 29 start-page: 442 year: 2011 ident: 9272_CR25 publication-title: Biotechnol. Adv. doi: 10.1016/j.biotechadv.2011.04.002 contributor: fullname: S Torres – volume: 160 start-page: 1909 year: 2010 ident: 9272_CR42 publication-title: Appl. Biochem. Biotechnol. doi: 10.1007/s12010-009-8702-0 contributor: fullname: P Prakash – volume: 70 start-page: 21 year: 2006 ident: 9272_CR8 publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-005-0239-8 contributor: fullname: R Gupta – volume: 79 start-page: 399 year: 2008 ident: 9272_CR22 publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-008-1429-y contributor: fullname: R Sareen – volume: 9 start-page: 60 year: 2008 ident: 9272_CR26 publication-title: J. Zhejiang Univ. Sci. B doi: 10.1631/jzus.B061620 contributor: fullname: CG Cai – volume: 34 start-page: 337 year: 2002 ident: 9272_CR41 publication-title: Lett. Appl. Microbiol. doi: 10.1046/j.1472-765X.2002.01093.x contributor: fullname: JD Allpress – volume-title: Molecular Cloning: A Laboratory Manual year: 2001 ident: 9272_CR14 contributor: fullname: J Sambrook – volume: 193 start-page: 265 year: 1951 ident: 9272_CR17 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)52451-6 contributor: fullname: OH Lowry |
SSID | ssj0002118237 |
Score | 2.2321734 |
Snippet | Feather waste, a by-product of poultry processing sectors, contains a large quantity of hard to degrade
keratin
that pose great threat to the environment and... |
SourceID | crossref springer |
SourceType | Aggregation Database Publisher |
StartPage | 595 |
SubjectTerms | Engineering Environment Environmental Engineering/Biotechnology Industrial Pollution Prevention Original Paper Renewable and Green Energy Waste Management/Waste Technology |
Title | Keratinolytic Protease Production by Bacillus amyloliquefaciens 6B Using Feather Meal as Substrate and Application of Feather Hydrolysate as Organic Nitrogen Input for Agricultural Soil |
URI | https://link.springer.com/article/10.1007/s12649-013-9272-5 |
Volume | 5 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV07T8MwELZou8DAG1FeuoEJFNTEeThjCq3Kq0IqSGyRHScoIiRV0wz9afw7zknaUgkGGCJ5ODlR7nz3ne_8mZBzYUemEyjjDQypmYK5Glc5DwYL18WkKAx5eXXCyBm-spueoskxFlsX6fvVvCJZOurlWTcM3aq1h2qu4WAC1SAtDD0W2nbL690NHhY7K4bCzCVZps4cR7Vw6fNy5k_zrAak1WpoGWT6W__5vG2yWUNK8Cob2CFrYbpLNr4RDe6Rz3vFnRynWTJDIXhS5AwYvtRAVvSxIGbQ5UGcJEUO_APT-EQxu0Zcrf0c7C6UzQVQQ0Z4RIAJPAfleEqCW-CpBG9ZDocsWggPZnKCr85LsRyq858BDOPpJEMDhtt0XEwB4TN4b5MFGQiMsjjZJy_93vP1QKsvbdACg7GpxkJbUjdwOx2BeXdIaWSKSHdohIlLJ5IIh3BoB-hJbGkpMjxhMs6sDhVSpxyfA9JMszQ8JGCbthRSOAIFTPyrqiIpucEZlY5r6HabXMw1548rbg5_ycKs9OGjPnylD99qk8u54vx6mea_Sx_9SfqYrCOOMqu-wBPSnE6K8JQ0clmc1cb5BSKw4Fk |
link.rule.ids | 315,782,786,27933,27934,41073,42142,48344,48347,48357,49649,49652,49662,52153 |
linkProvider | Springer Nature |
linkToHtml | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1NT9tAEB014dByKKUtAgrtHHpqZSn2Ovb6GBpQECRCgkrJydr12siSsVGcHPLT-HfM-CNpJHqAg6U9jGzLMzvzxjPzFuCn9hLXj9h4I8dYrpaBpTjnoWARBJQUxbGqjk649SdTOTxnmhzRzsJU3e5tSbLy1JthN4rd3NsjrMDxKYPqwA6TnTtd2BlMZ7Ph-teKw6C5Ysu0pe9zD5fd1jNfus92RNouh1ZR5mLvTe_3CT42oBIHtRXsw7s4_wy7_1ANfoGnK2ZPTvMiW5EQ3jA9AwUwXpiaQBb1Cs9UlGbZskT1QIl8xtyuieLdX6J3hlV7ATagEccEMVGVyK6norhFlRscbAriWCRr4dHKzOnRZSVWYj0BGuEkXcwLMmG8zB-XCyQAjYP7-ZoOBG-LNPsKfy_O7_6MrObYBitypFxYMvaMCKKg19OUecdCJK5ObF8klLr0EkOAiJZeRL7EM32mw9OuVLLfE9rYQtF1AN28yONDQM_1jDba1yTg0lflmqRRjpLC-IFje0fwq1Vd-Fizc4QbHmbWR0j6CFkfYf8IfreKC5uNWv5f-vhV0j_g_ehufB1eX06uvsEHQlVu3SV4At3FfBmfQqc0y--NpT4D8H7kiw |
linkToPdf | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LT9tAEB6VICE4QClUhJYyh56KLOJH7PUJBUhKRBtFSpC4Wbteu4pk7Ch2Dvlp_Dtm_EiKBIeqB0t7GNmWZzzzzc7MtwDflRs7XsjGG1racJTwDck5DwUL36ekKIpkeXTCxBs9its-0-RcNbMwZbd7U5KsZhqYpSktLuc6vtwMvlEc5z4f2_Atj7KpLdjmXTGnBdu94fTnYL3NYjGALpkzTeF53M9lNrXNt-7zOjq9Lo2WEWdw8N_v-hH2a7CJvco6DuFDlH6Cvb8oCI_g-Z5ZlWdplqxICMdM20CBjRe6IpZFtcJrGc6SZJmjfKIEP2HO11iyV8jRvcay7QBrMIm_CXqizJFdUkl9izLV2NsUyjGL18J3K72gR-elWI7VZGiIo1mxyMi0cZjOlwUSsMben8WaJgQn2Sw5hodBf3pzZ9THORihJURhiMjVth_6nY6ijDyy7dhRsenZMaU0nVgTUKKlG5KPcXWXafKUI6TodmylTVvS9RlaaZZGJ4Cu42qlladIwKGvyrVKLS0pbO35lum24UejxmBesXYEG35m1kdA-ghYH0G3DReNEoP6B87flz79J-lz2BnfDoJfw9H9F9glsOVUzYNfoVUsltEZbOV6-a022hcCL-0i |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Keratinolytic+Protease+Production+by+Bacillus+amyloliquefaciens+6B+Using+Feather+Meal+as+Substrate+and+Application+of+Feather+Hydrolysate+as+Organic+Nitrogen+Input+for+Agricultural+Soil&rft.jtitle=Waste+and+biomass+valorization&rft.au=Bose%2C+Anjali&rft.au=Pathan%2C+Shabnam&rft.au=Pathak%2C+Khyati&rft.au=Keharia%2C+Haresh&rft.date=2014-08-01&rft.pub=Springer+Netherlands&rft.issn=1877-2641&rft.eissn=1877-265X&rft.volume=5&rft.issue=4&rft.spage=595&rft.epage=605&rft_id=info:doi/10.1007%2Fs12649-013-9272-5&rft.externalDocID=10_1007_s12649_013_9272_5 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1877-2641&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1877-2641&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1877-2641&client=summon |