Structure and biotechnological applications of odorant-binding proteins
Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are...
Gespeichert in:
Veröffentlicht in: | Applied microbiology and biotechnology 2014-01, Vol.98 (1), p.61-70 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 70 |
---|---|
container_issue | 1 |
container_start_page | 61 |
container_title | Applied microbiology and biotechnology |
container_volume | 98 |
creator | Pelosi, Paolo Mastrogiacomo, Rosa Iovinella, Immacolata Tuccori, Elena Persaud, Krishna C. |
description | Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are folded into α-helical domains. Both types of architectures are extremely stable to temperature, organic solvents and proteolytic digestion. These characteristics make OBPs suitable elements for fabricating biosensors to be used in the environment, as well as for other biotechnological applications. The affinity of OBPs for small volatile organic compounds is in the micromolar range, and they have broad specificity to a range of ligands. For biotechnological applications, OBPs can be expressed in bacterial systems at low cost and are easily purified. The large amount of information available on their structures and affinities to different molecules should allow the design of specific mutants with desired characteristics and represent a solid base for tailoring OBPs for different applications. |
doi_str_mv | 10.1007/s00253-013-5383-y |
format | Article |
fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_1753555167</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A357759843</galeid><sourcerecordid>A357759843</sourcerecordid><originalsourceid>FETCH-LOGICAL-c646t-9430838a3f0b16f49699b4c9439b71a4334a313898c49e8ab3144d72ffdabc923</originalsourceid><addsrcrecordid>eNqNksFrFDEYxYModrv6B3iRAS_2MDXJl2SSYylaCwXB6jlkMpkxZTZZkwx0_3uzbJWuKEoOCV9-74VHHkKvCD4nGHfvMsaUQ4sJtBwktLsnaEUY0BYLwp6iFSYdbzuu5Ak6zfkOY0KlEM_RCWVUcAx4ha5uS1psWZJrTBia3sfi7LcQ5zh5a-bGbLdzPRQfQ27i2MQhJhNK2_sw-DA121QFPuQX6Nlo5uxePuxr9PXD-y-XH9ubT1fXlxc3rRVMlFYxwBKkgRH3RIxMCaV6ZutY9R0xDIAZICCVtEw5aXogjA0dHcfB9FZRWKO3B9_68PfF5aI3Pls3zya4uGRdEwPnnIju3yhTVOCKqv9BcScFkaSib35D7-KSQs1cqQ4ACwaPqMnMTvswxpKM3ZvqC-Dd_k9q1jU6_wNV1-A23sbgRl_nR4KzI0Flirsvk1ly1te3n49ZcmBtijknN-pt8huTdppgva-PPtRH1_rofX30rmpeP4Rb-o0bfil-9qUC9ADkehUmlx6l_6vrDxRTy8E</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1473306431</pqid></control><display><type>article</type><title>Structure and biotechnological applications of odorant-binding proteins</title><source>MEDLINE</source><source>SpringerNature Journals</source><creator>Pelosi, Paolo ; Mastrogiacomo, Rosa ; Iovinella, Immacolata ; Tuccori, Elena ; Persaud, Krishna C.</creator><creatorcontrib>Pelosi, Paolo ; Mastrogiacomo, Rosa ; Iovinella, Immacolata ; Tuccori, Elena ; Persaud, Krishna C.</creatorcontrib><description>Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are folded into α-helical domains. Both types of architectures are extremely stable to temperature, organic solvents and proteolytic digestion. These characteristics make OBPs suitable elements for fabricating biosensors to be used in the environment, as well as for other biotechnological applications. The affinity of OBPs for small volatile organic compounds is in the micromolar range, and they have broad specificity to a range of ligands. For biotechnological applications, OBPs can be expressed in bacterial systems at low cost and are easily purified. The large amount of information available on their structures and affinities to different molecules should allow the design of specific mutants with desired characteristics and represent a solid base for tailoring OBPs for different applications.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-013-5383-y</identifier><identifier>PMID: 24265030</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Affinity ; Amino Acid Sequence ; Amino acids ; Animals ; Bacteria ; Binding proteins ; Biomedical and Life Sciences ; Biosensing Techniques - methods ; Biosensors ; Biotechnology ; Biotechnology - methods ; Chemical properties ; Chemosensory perception ; Digestion ; Gene expression ; Genetic aspects ; Insecta ; Insects ; Life Sciences ; Ligands ; Microbial Genetics and Genomics ; Microbiology ; Mini-Review ; Models, Molecular ; Mutant Proteins - genetics ; Mutant Proteins - isolation & purification ; Mutant Proteins - metabolism ; Natural products ; Nose ; Organic compounds ; Organic solvents ; Pheromones ; Physiological aspects ; Polypeptides ; Protein Binding ; Protein Conformation ; Protein Stability ; Proteins ; Receptors, Odorant - chemistry ; Receptors, Odorant - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Software ; Studies ; Technology application ; Tissue engineering ; Vertebrates ; VOCs ; Volatile organic compounds ; Volatile Organic Compounds - metabolism</subject><ispartof>Applied microbiology and biotechnology, 2014-01, Vol.98 (1), p.61-70</ispartof><rights>Springer-Verlag Berlin Heidelberg 2013</rights><rights>COPYRIGHT 2014 Springer</rights><rights>Springer-Verlag Berlin Heidelberg 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c646t-9430838a3f0b16f49699b4c9439b71a4334a313898c49e8ab3144d72ffdabc923</citedby><cites>FETCH-LOGICAL-c646t-9430838a3f0b16f49699b4c9439b71a4334a313898c49e8ab3144d72ffdabc923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-013-5383-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-013-5383-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24265030$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pelosi, Paolo</creatorcontrib><creatorcontrib>Mastrogiacomo, Rosa</creatorcontrib><creatorcontrib>Iovinella, Immacolata</creatorcontrib><creatorcontrib>Tuccori, Elena</creatorcontrib><creatorcontrib>Persaud, Krishna C.</creatorcontrib><title>Structure and biotechnological applications of odorant-binding proteins</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are folded into α-helical domains. Both types of architectures are extremely stable to temperature, organic solvents and proteolytic digestion. These characteristics make OBPs suitable elements for fabricating biosensors to be used in the environment, as well as for other biotechnological applications. The affinity of OBPs for small volatile organic compounds is in the micromolar range, and they have broad specificity to a range of ligands. For biotechnological applications, OBPs can be expressed in bacterial systems at low cost and are easily purified. The large amount of information available on their structures and affinities to different molecules should allow the design of specific mutants with desired characteristics and represent a solid base for tailoring OBPs for different applications.</description><subject>Affinity</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Bacteria</subject><subject>Binding proteins</subject><subject>Biomedical and Life Sciences</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensors</subject><subject>Biotechnology</subject><subject>Biotechnology - methods</subject><subject>Chemical properties</subject><subject>Chemosensory perception</subject><subject>Digestion</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>Insecta</subject><subject>Insects</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mini-Review</subject><subject>Models, Molecular</subject><subject>Mutant Proteins - genetics</subject><subject>Mutant Proteins - isolation & purification</subject><subject>Mutant Proteins - metabolism</subject><subject>Natural products</subject><subject>Nose</subject><subject>Organic compounds</subject><subject>Organic solvents</subject><subject>Pheromones</subject><subject>Physiological aspects</subject><subject>Polypeptides</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Stability</subject><subject>Proteins</subject><subject>Receptors, Odorant - chemistry</subject><subject>Receptors, Odorant - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Software</subject><subject>Studies</subject><subject>Technology application</subject><subject>Tissue engineering</subject><subject>Vertebrates</subject><subject>VOCs</subject><subject>Volatile organic compounds</subject><subject>Volatile Organic Compounds - metabolism</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNksFrFDEYxYModrv6B3iRAS_2MDXJl2SSYylaCwXB6jlkMpkxZTZZkwx0_3uzbJWuKEoOCV9-74VHHkKvCD4nGHfvMsaUQ4sJtBwktLsnaEUY0BYLwp6iFSYdbzuu5Ak6zfkOY0KlEM_RCWVUcAx4ha5uS1psWZJrTBia3sfi7LcQ5zh5a-bGbLdzPRQfQ27i2MQhJhNK2_sw-DA121QFPuQX6Nlo5uxePuxr9PXD-y-XH9ubT1fXlxc3rRVMlFYxwBKkgRH3RIxMCaV6ZutY9R0xDIAZICCVtEw5aXogjA0dHcfB9FZRWKO3B9_68PfF5aI3Pls3zya4uGRdEwPnnIju3yhTVOCKqv9BcScFkaSib35D7-KSQs1cqQ4ACwaPqMnMTvswxpKM3ZvqC-Dd_k9q1jU6_wNV1-A23sbgRl_nR4KzI0Flirsvk1ly1te3n49ZcmBtijknN-pt8huTdppgva-PPtRH1_rofX30rmpeP4Rb-o0bfil-9qUC9ADkehUmlx6l_6vrDxRTy8E</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Pelosi, Paolo</creator><creator>Mastrogiacomo, Rosa</creator><creator>Iovinella, Immacolata</creator><creator>Tuccori, Elena</creator><creator>Persaud, Krishna C.</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope><scope>7QR</scope><scope>7U5</scope><scope>F28</scope><scope>L7M</scope></search><sort><creationdate>20140101</creationdate><title>Structure and biotechnological applications of odorant-binding proteins</title><author>Pelosi, Paolo ; Mastrogiacomo, Rosa ; Iovinella, Immacolata ; Tuccori, Elena ; Persaud, Krishna C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c646t-9430838a3f0b16f49699b4c9439b71a4334a313898c49e8ab3144d72ffdabc923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Affinity</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Bacteria</topic><topic>Binding proteins</topic><topic>Biomedical and Life Sciences</topic><topic>Biosensing Techniques - methods</topic><topic>Biosensors</topic><topic>Biotechnology</topic><topic>Biotechnology - methods</topic><topic>Chemical properties</topic><topic>Chemosensory perception</topic><topic>Digestion</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>Insecta</topic><topic>Insects</topic><topic>Life Sciences</topic><topic>Ligands</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mini-Review</topic><topic>Models, Molecular</topic><topic>Mutant Proteins - genetics</topic><topic>Mutant Proteins - isolation & purification</topic><topic>Mutant Proteins - metabolism</topic><topic>Natural products</topic><topic>Nose</topic><topic>Organic compounds</topic><topic>Organic solvents</topic><topic>Pheromones</topic><topic>Physiological aspects</topic><topic>Polypeptides</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Stability</topic><topic>Proteins</topic><topic>Receptors, Odorant - chemistry</topic><topic>Receptors, Odorant - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Software</topic><topic>Studies</topic><topic>Technology application</topic><topic>Tissue engineering</topic><topic>Vertebrates</topic><topic>VOCs</topic><topic>Volatile organic compounds</topic><topic>Volatile Organic Compounds - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pelosi, Paolo</creatorcontrib><creatorcontrib>Mastrogiacomo, Rosa</creatorcontrib><creatorcontrib>Iovinella, Immacolata</creatorcontrib><creatorcontrib>Tuccori, Elena</creatorcontrib><creatorcontrib>Persaud, Krishna C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Access via ABI/INFORM (ProQuest)</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pelosi, Paolo</au><au>Mastrogiacomo, Rosa</au><au>Iovinella, Immacolata</au><au>Tuccori, Elena</au><au>Persaud, Krishna C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and biotechnological applications of odorant-binding proteins</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>98</volume><issue>1</issue><spage>61</spage><epage>70</epage><pages>61-70</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are folded into α-helical domains. Both types of architectures are extremely stable to temperature, organic solvents and proteolytic digestion. These characteristics make OBPs suitable elements for fabricating biosensors to be used in the environment, as well as for other biotechnological applications. The affinity of OBPs for small volatile organic compounds is in the micromolar range, and they have broad specificity to a range of ligands. For biotechnological applications, OBPs can be expressed in bacterial systems at low cost and are easily purified. The large amount of information available on their structures and affinities to different molecules should allow the design of specific mutants with desired characteristics and represent a solid base for tailoring OBPs for different applications.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>24265030</pmid><doi>10.1007/s00253-013-5383-y</doi><tpages>10</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0175-7598 |
ispartof | Applied microbiology and biotechnology, 2014-01, Vol.98 (1), p.61-70 |
issn | 0175-7598 1432-0614 |
language | eng |
recordid | cdi_proquest_miscellaneous_1753555167 |
source | MEDLINE; SpringerNature Journals |
subjects | Affinity Amino Acid Sequence Amino acids Animals Bacteria Binding proteins Biomedical and Life Sciences Biosensing Techniques - methods Biosensors Biotechnology Biotechnology - methods Chemical properties Chemosensory perception Digestion Gene expression Genetic aspects Insecta Insects Life Sciences Ligands Microbial Genetics and Genomics Microbiology Mini-Review Models, Molecular Mutant Proteins - genetics Mutant Proteins - isolation & purification Mutant Proteins - metabolism Natural products Nose Organic compounds Organic solvents Pheromones Physiological aspects Polypeptides Protein Binding Protein Conformation Protein Stability Proteins Receptors, Odorant - chemistry Receptors, Odorant - metabolism Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Software Studies Technology application Tissue engineering Vertebrates VOCs Volatile organic compounds Volatile Organic Compounds - metabolism |
title | Structure and biotechnological applications of odorant-binding proteins |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-22T13%3A29%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20and%20biotechnological%20applications%20of%20odorant-binding%20proteins&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Pelosi,%20Paolo&rft.date=2014-01-01&rft.volume=98&rft.issue=1&rft.spage=61&rft.epage=70&rft.pages=61-70&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/10.1007/s00253-013-5383-y&rft_dat=%3Cgale_proqu%3EA357759843%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1473306431&rft_id=info:pmid/24265030&rft_galeid=A357759843&rfr_iscdi=true |