The effect of microwave on the interaction of flavour compounds with G‐actin from grass carp (Catenopharyngodon idella)

BACKGROUND In order to investigate the influence of non‐thermal effects of microwaves on the flavour of fish and meat products, the G‐actin of grass carp in ice baths was exposed to different microwave powers (0, 100, 300 or 500 W); the surface hydrophobicity, sulfhydryl contents, secondary structur...

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Veröffentlicht in:Journal of the science of food and agriculture 2017-09, Vol.97 (12), p.3917-3922
Hauptverfasser: Lou, Xiaowei, Yang, Qiuli, Sun, Yangying, Pan, Daodong, Cao, Jinxuan
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container_end_page 3922
container_issue 12
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container_title Journal of the science of food and agriculture
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creator Lou, Xiaowei
Yang, Qiuli
Sun, Yangying
Pan, Daodong
Cao, Jinxuan
description BACKGROUND In order to investigate the influence of non‐thermal effects of microwaves on the flavour of fish and meat products, the G‐actin of grass carp in ice baths was exposed to different microwave powers (0, 100, 300 or 500 W); the surface hydrophobicity, sulfhydryl contents, secondary structures and adsorption capacity of G‐actin to ketones were determined. RESULTS As microwave power increased from 0 to 300 W, the surface hydrophobicity, total and reactive sulfhydryls increased; α‐helix, β‐sheet and random coil fractions turned into β‐turn fractions. As microwave power increased from 300 to 500 W, however, hydrophobicity and sulfhydryl contents decreased; β‐turn and random coil fractions turned into α‐helix and β‐sheet fractions. The tendencies of adsorbed capacity of ketones were similar to hydrophobicity and sulfhydryl contents. CONCLUSION The increased adsorbing of ketones could be attributed to the unfolding of secondary structures by revealing new binding sites, including thiol groups and hydrophobic binding sites. The decreased binding capacity was related to the refolding and aggregation of protein. The results suggested that microwave powers had obvious effects on the flavour retention and proteins structures in muscle foods. © 2017 Society of Chemical Industry
doi_str_mv 10.1002/jsfa.8325
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RESULTS As microwave power increased from 0 to 300 W, the surface hydrophobicity, total and reactive sulfhydryls increased; α‐helix, β‐sheet and random coil fractions turned into β‐turn fractions. As microwave power increased from 300 to 500 W, however, hydrophobicity and sulfhydryl contents decreased; β‐turn and random coil fractions turned into α‐helix and β‐sheet fractions. The tendencies of adsorbed capacity of ketones were similar to hydrophobicity and sulfhydryl contents. CONCLUSION The increased adsorbing of ketones could be attributed to the unfolding of secondary structures by revealing new binding sites, including thiol groups and hydrophobic binding sites. The decreased binding capacity was related to the refolding and aggregation of protein. The results suggested that microwave powers had obvious effects on the flavour retention and proteins structures in muscle foods. © 2017 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.8325</identifier><identifier>PMID: 28345129</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>Actin ; Actins - chemistry ; Adsorption ; Agglomeration ; Animals ; Aroma compounds ; Binding sites ; Carp ; Carps ; Coils ; Fish Proteins - chemistry ; Flavor compounds ; Flavoring Agents - chemistry ; Food ; G‐actin ; Hydrophobic and Hydrophilic Interactions - radiation effects ; Hydrophobicity ; Ice ; Ketones ; Ketones - chemistry ; Meat ; Meat products ; microwave treatment ; Microwaves ; Protein folding ; Protein Folding - radiation effects ; protein structure ; Protein Structure, Secondary - radiation effects ; Proteins ; Random coil ; Surface chemistry ; Temperature effects ; volatile compound</subject><ispartof>Journal of the science of food and agriculture, 2017-09, Vol.97 (12), p.3917-3922</ispartof><rights>2017 Society of Chemical Industry</rights><rights>2017 Society of Chemical Industry.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3535-d4a4b8faa84c68c7730dfcba7c5005c8739e56f69df9bc8aa3fd25f17f1fb58b3</citedby><cites>FETCH-LOGICAL-c3535-d4a4b8faa84c68c7730dfcba7c5005c8739e56f69df9bc8aa3fd25f17f1fb58b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.8325$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.8325$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,782,786,1419,27931,27932,45581,45582</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28345129$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lou, Xiaowei</creatorcontrib><creatorcontrib>Yang, Qiuli</creatorcontrib><creatorcontrib>Sun, Yangying</creatorcontrib><creatorcontrib>Pan, Daodong</creatorcontrib><creatorcontrib>Cao, Jinxuan</creatorcontrib><title>The effect of microwave on the interaction of flavour compounds with G‐actin from grass carp (Catenopharyngodon idella)</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>BACKGROUND In order to investigate the influence of non‐thermal effects of microwaves on the flavour of fish and meat products, the G‐actin of grass carp in ice baths was exposed to different microwave powers (0, 100, 300 or 500 W); the surface hydrophobicity, sulfhydryl contents, secondary structures and adsorption capacity of G‐actin to ketones were determined. RESULTS As microwave power increased from 0 to 300 W, the surface hydrophobicity, total and reactive sulfhydryls increased; α‐helix, β‐sheet and random coil fractions turned into β‐turn fractions. As microwave power increased from 300 to 500 W, however, hydrophobicity and sulfhydryl contents decreased; β‐turn and random coil fractions turned into α‐helix and β‐sheet fractions. The tendencies of adsorbed capacity of ketones were similar to hydrophobicity and sulfhydryl contents. CONCLUSION The increased adsorbing of ketones could be attributed to the unfolding of secondary structures by revealing new binding sites, including thiol groups and hydrophobic binding sites. The decreased binding capacity was related to the refolding and aggregation of protein. 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the surface hydrophobicity, sulfhydryl contents, secondary structures and adsorption capacity of G‐actin to ketones were determined. RESULTS As microwave power increased from 0 to 300 W, the surface hydrophobicity, total and reactive sulfhydryls increased; α‐helix, β‐sheet and random coil fractions turned into β‐turn fractions. As microwave power increased from 300 to 500 W, however, hydrophobicity and sulfhydryl contents decreased; β‐turn and random coil fractions turned into α‐helix and β‐sheet fractions. The tendencies of adsorbed capacity of ketones were similar to hydrophobicity and sulfhydryl contents. CONCLUSION The increased adsorbing of ketones could be attributed to the unfolding of secondary structures by revealing new binding sites, including thiol groups and hydrophobic binding sites. The decreased binding capacity was related to the refolding and aggregation of protein. The results suggested that microwave powers had obvious effects on the flavour retention and proteins structures in muscle foods. © 2017 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>28345129</pmid><doi>10.1002/jsfa.8325</doi><tpages>6</tpages></addata></record>
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subjects Actin
Actins - chemistry
Adsorption
Agglomeration
Animals
Aroma compounds
Binding sites
Carp
Carps
Coils
Fish Proteins - chemistry
Flavor compounds
Flavoring Agents - chemistry
Food
G‐actin
Hydrophobic and Hydrophilic Interactions - radiation effects
Hydrophobicity
Ice
Ketones
Ketones - chemistry
Meat
Meat products
microwave treatment
Microwaves
Protein folding
Protein Folding - radiation effects
protein structure
Protein Structure, Secondary - radiation effects
Proteins
Random coil
Surface chemistry
Temperature effects
volatile compound
title The effect of microwave on the interaction of flavour compounds with G‐actin from grass carp (Catenopharyngodon idella)
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