Thermal and single frequency counter-current ultrasound pretreatments of sodium caseinate: enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution and antioxidant peptides

BACKGROUND Due to the disadvantages of traditional enzymolysis, pretreatments are crucial to enhance protein enzymolysis. Enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution, fluorescence spectroscopy and antioxidant activity of thermal (HT) and single fre...

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Veröffentlicht in:Journal of the science of food and agriculture 2016-12, Vol.96 (15), p.4861-4873
Hauptverfasser: Abdualrahman, Mohammed Adam Y, Ma, Haile, Zhou, Cunshan, Yagoub, Abu ElGasim A, Hu, Jiali, Yang, Xue
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container_issue 15
container_start_page 4861
container_title Journal of the science of food and agriculture
container_volume 96
creator Abdualrahman, Mohammed Adam Y
Ma, Haile
Zhou, Cunshan
Yagoub, Abu ElGasim A
Hu, Jiali
Yang, Xue
description BACKGROUND Due to the disadvantages of traditional enzymolysis, pretreatments are crucial to enhance protein enzymolysis. Enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution, fluorescence spectroscopy and antioxidant activity of thermal (HT) and single frequency counter‐current ultrasound (SCFU) pretreated sodium caseinate (NaCas) were studied. RESULTS Enzymolysis of untreated NaCas (control) improved significantly (P < 0.05) by SFCU and followed by HT. Values of the Michaelis–Menten constant (KM) of SFCU and HT were 0.0212 and 0.0250, respectively. HT and SFCU increased (P < 0.05) the reaction rate constant (k) by 38.64 and 90.91%, respectively at 298 K. k values decreased with increasing temperature. The initial activation energy (46.39 kJ mol−1) reduced (P < 0.05) by HT (39.66 kJ mol−1) and further by SFCU (33.42 kJ mol−1). SFCU‐pretreated NaCas hydrolysates had the highest contents of hydrophobic, aromatic, positively and negatively charged amino acids. Medium‐sized peptides (5000–1000 Da) are higher in SFCU (78.11%) than HT and the control. SFCU induced molecular unfolding of NaCas proteins. Accordingly, SFCU‐pretreated NaCas hydrolysate exhibited the highest scavenging activity on DPPH and hydroxyl radicals, reducing power, and iron chelating ability. CONCLUSION SFCU pretreatment would be a useful tool for production of bioactive peptides from NaCas hydrolysate. © 2016 Society of Chemical Industry
doi_str_mv 10.1002/jsfa.7996
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Enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution, fluorescence spectroscopy and antioxidant activity of thermal (HT) and single frequency counter‐current ultrasound (SCFU) pretreated sodium caseinate (NaCas) were studied. RESULTS Enzymolysis of untreated NaCas (control) improved significantly (P &lt; 0.05) by SFCU and followed by HT. Values of the Michaelis–Menten constant (KM) of SFCU and HT were 0.0212 and 0.0250, respectively. HT and SFCU increased (P &lt; 0.05) the reaction rate constant (k) by 38.64 and 90.91%, respectively at 298 K. k values decreased with increasing temperature. The initial activation energy (46.39 kJ mol−1) reduced (P &lt; 0.05) by HT (39.66 kJ mol−1) and further by SFCU (33.42 kJ mol−1). SFCU‐pretreated NaCas hydrolysates had the highest contents of hydrophobic, aromatic, positively and negatively charged amino acids. Medium‐sized peptides (5000–1000 Da) are higher in SFCU (78.11%) than HT and the control. SFCU induced molecular unfolding of NaCas proteins. Accordingly, SFCU‐pretreated NaCas hydrolysate exhibited the highest scavenging activity on DPPH and hydroxyl radicals, reducing power, and iron chelating ability. CONCLUSION SFCU pretreatment would be a useful tool for production of bioactive peptides from NaCas hydrolysate. © 2016 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.7996</identifier><identifier>PMID: 27539674</identifier><identifier>CODEN: JSFAAE</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>Amino acids ; Amino Acids - analysis ; amino acids composition ; antioxidant activity ; Antioxidants ; Caseins - chemistry ; Caseins - metabolism ; enzymolysis kinetic ; Free Radicals - chemistry ; Heat treatment ; Hydrolysates ; Hydrolysis ; Iron Chelating Agents - chemistry ; Kinetics ; Molecular Weight ; Molecular weight distribution ; Peptides ; Peptides - chemistry ; Pretreatment ; Protein Conformation ; Proteins ; Sodium ; sodium caseinate ; Spectrometry, Fluorescence ; thermal and ultrasound pretreatments ; Thermodynamics ; Ultrasonic imaging ; Ultrasonic Waves</subject><ispartof>Journal of the science of food and agriculture, 2016-12, Vol.96 (15), p.4861-4873</ispartof><rights>2016 Society of Chemical Industry</rights><rights>2016 Society of Chemical Industry.</rights><rights>Copyright © 2016 Society of Chemical Industry</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4576-f84c585912d100cebce5a38671726fe871c11d78b0304c9770c96d8f69c405603</citedby><cites>FETCH-LOGICAL-c4576-f84c585912d100cebce5a38671726fe871c11d78b0304c9770c96d8f69c405603</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.7996$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.7996$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27539674$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abdualrahman, Mohammed Adam Y</creatorcontrib><creatorcontrib>Ma, Haile</creatorcontrib><creatorcontrib>Zhou, Cunshan</creatorcontrib><creatorcontrib>Yagoub, Abu ElGasim A</creatorcontrib><creatorcontrib>Hu, Jiali</creatorcontrib><creatorcontrib>Yang, Xue</creatorcontrib><title>Thermal and single frequency counter-current ultrasound pretreatments of sodium caseinate: enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution and antioxidant peptides</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>BACKGROUND Due to the disadvantages of traditional enzymolysis, pretreatments are crucial to enhance protein enzymolysis. Enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution, fluorescence spectroscopy and antioxidant activity of thermal (HT) and single frequency counter‐current ultrasound (SCFU) pretreated sodium caseinate (NaCas) were studied. RESULTS Enzymolysis of untreated NaCas (control) improved significantly (P &lt; 0.05) by SFCU and followed by HT. Values of the Michaelis–Menten constant (KM) of SFCU and HT were 0.0212 and 0.0250, respectively. HT and SFCU increased (P &lt; 0.05) the reaction rate constant (k) by 38.64 and 90.91%, respectively at 298 K. k values decreased with increasing temperature. The initial activation energy (46.39 kJ mol−1) reduced (P &lt; 0.05) by HT (39.66 kJ mol−1) and further by SFCU (33.42 kJ mol−1). SFCU‐pretreated NaCas hydrolysates had the highest contents of hydrophobic, aromatic, positively and negatively charged amino acids. Medium‐sized peptides (5000–1000 Da) are higher in SFCU (78.11%) than HT and the control. SFCU induced molecular unfolding of NaCas proteins. Accordingly, SFCU‐pretreated NaCas hydrolysate exhibited the highest scavenging activity on DPPH and hydroxyl radicals, reducing power, and iron chelating ability. 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Sci. Food Agric</addtitle><date>2016-12</date><risdate>2016</risdate><volume>96</volume><issue>15</issue><spage>4861</spage><epage>4873</epage><pages>4861-4873</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><coden>JSFAAE</coden><abstract>BACKGROUND Due to the disadvantages of traditional enzymolysis, pretreatments are crucial to enhance protein enzymolysis. Enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution, fluorescence spectroscopy and antioxidant activity of thermal (HT) and single frequency counter‐current ultrasound (SCFU) pretreated sodium caseinate (NaCas) were studied. RESULTS Enzymolysis of untreated NaCas (control) improved significantly (P &lt; 0.05) by SFCU and followed by HT. Values of the Michaelis–Menten constant (KM) of SFCU and HT were 0.0212 and 0.0250, respectively. HT and SFCU increased (P &lt; 0.05) the reaction rate constant (k) by 38.64 and 90.91%, respectively at 298 K. k values decreased with increasing temperature. The initial activation energy (46.39 kJ mol−1) reduced (P &lt; 0.05) by HT (39.66 kJ mol−1) and further by SFCU (33.42 kJ mol−1). SFCU‐pretreated NaCas hydrolysates had the highest contents of hydrophobic, aromatic, positively and negatively charged amino acids. Medium‐sized peptides (5000–1000 Da) are higher in SFCU (78.11%) than HT and the control. SFCU induced molecular unfolding of NaCas proteins. Accordingly, SFCU‐pretreated NaCas hydrolysate exhibited the highest scavenging activity on DPPH and hydroxyl radicals, reducing power, and iron chelating ability. CONCLUSION SFCU pretreatment would be a useful tool for production of bioactive peptides from NaCas hydrolysate. © 2016 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>27539674</pmid><doi>10.1002/jsfa.7996</doi><tpages>13</tpages></addata></record>
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subjects Amino acids
Amino Acids - analysis
amino acids composition
antioxidant activity
Antioxidants
Caseins - chemistry
Caseins - metabolism
enzymolysis kinetic
Free Radicals - chemistry
Heat treatment
Hydrolysates
Hydrolysis
Iron Chelating Agents - chemistry
Kinetics
Molecular Weight
Molecular weight distribution
Peptides
Peptides - chemistry
Pretreatment
Protein Conformation
Proteins
Sodium
sodium caseinate
Spectrometry, Fluorescence
thermal and ultrasound pretreatments
Thermodynamics
Ultrasonic imaging
Ultrasonic Waves
title Thermal and single frequency counter-current ultrasound pretreatments of sodium caseinate: enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution and antioxidant peptides
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