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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Applied microbiology and biotechnology 2014-01, Vol.98 (1), p.61-70
Hauptverfasser: Pelosi, Paolo, Mastrogiacomo, Rosa, Iovinella, Immacolata, Tuccori, Elena, Persaud, Krishna C.
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 &amp; 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 &amp; 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 &amp; 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 &amp; 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 &amp; 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 &amp; 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 &amp; 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 &amp; Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health &amp; 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 &amp; 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