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Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid ( Dosidicus gigas ) Mantle Muscle
Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid ( ) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC...
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| Published in: | Food technology and biotechnology 2019-01, Vol.57 (1), p.39-47 |
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| container_title | Food technology and biotechnology |
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| creator | Álvarez-Armenta, Andrés Carvajal-Millán, Elizabeth Pacheco-Aguilar, Ramón García-Sánchez, Guillermina Márquez-Ríos, Enrique Scheuren-Acevedo, Susana María Ramírez-Suárez, Juan Carlos |
| description | Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid (
) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC ( |
| doi_str_mv | 10.17113/ftb.57.01.19.5848 |
| format | article |
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) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC (<1 kDa) fraction obtained from jumbo squid muscle was evaluated by Fourier transform infrared spectrometry. From its spectra, total carbohydrates, free monosaccharides, free amino acids and ammonium chloride were determined. Cryoprotectant capacity and protein cryostability conferred by LMMC were investigated by differential scanning calorimetry. Fraction partial characterization showed that the main components are free amino acids (18.84 mg/g), carbohydrates (67.1 µg/mg) such as monosaccharides (51.1 µg/mg of glucose, fucose and arabinose in total) and ammonium chloride (220.4 µg/mg). Arginine, sarcosine and taurine were the main amino acids in the fraction. LMMC, at the mass fraction present in jumbo squid muscle, lowered the water freezing point to -1.2 °C, inhibiting recrystallization at 0.66 °C. Significant myofibrillar protein stabilization by LMMC was observed after a freeze-thaw cycle compared to control (muscle after extraction of LMMC), proving the effectiveness on jumbo squid protein muscle cryo- stability. Osmolytes in LMMC fraction inhibited protein denaturation/aggregation and ice recrystallization, maintaining the muscle structure stable under freezing conditions. LMMC conferred protein cryostability even at the very low mass fraction in the muscle.</description><identifier>ISSN: 1330-9862</identifier><identifier>EISSN: 1334-2606</identifier><identifier>DOI: 10.17113/ftb.57.01.19.5848</identifier><identifier>PMID: 31316275</identifier><language>eng</language><publisher>Croatia: Sveuciliste U Zagrebu</publisher><subject>Agglomeration ; Amino acids ; Ammonium ; Ammonium chloride ; Ammonium salts ; Arabinose ; Arginine ; Biopolymer denaturation ; Calorimetry ; Carbohydrates ; Cryoprotectants ; Cryoprotectors ; cryostability ; Differential scanning calorimetry ; Dosidicus gigas ; Fish ; Food ; Fourier transforms ; free amino acids ; Freeze thaw cycles ; Freeze-thawing ; Freezing ; Freezing point ; Fucose ; Glucose ; Handbooks ; Infrared spectra ; Infrared spectroscopy ; Melting points ; Monosaccharides ; Muscles ; myofibrillar protein ; Original Scientific Papers ; Phase transitions ; Protein denaturation ; Protein folding ; Proteins ; Recrystallization ; Sarcosine ; Spectrometry ; Spectroscopy ; Squid ; squid muscle ; Studies ; Taurine ; Water</subject><ispartof>Food technology and biotechnology, 2019-01, Vol.57 (1), p.39-47</ispartof><rights>COPYRIGHT 2019 Sveuciliste U Zagrebu</rights><rights>2019. This work is published under https://creativecommons.org/licenses/by-nc/4.0 (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 University of Zagreb Faculty of Food Technology and Biotechnology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c535t-656e7985c173283cd960e559dc5f86b268e6c79e1d07a963bacbf29b84eefd93</citedby><orcidid>0000-0002-1669-8007 ; 0000-0001-5801-4593 ; 0000-0001-8512-1271 ; 0000-0003-4390-7457 ; 0000-0003-3748-0530 ; 0000-0001-8907-947X ; 0000-0001-7850-4960</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2212666984/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2212666984?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768,74869</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31316275$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Álvarez-Armenta, Andrés</creatorcontrib><creatorcontrib>Carvajal-Millán, Elizabeth</creatorcontrib><creatorcontrib>Pacheco-Aguilar, Ramón</creatorcontrib><creatorcontrib>García-Sánchez, Guillermina</creatorcontrib><creatorcontrib>Márquez-Ríos, Enrique</creatorcontrib><creatorcontrib>Scheuren-Acevedo, Susana María</creatorcontrib><creatorcontrib>Ramírez-Suárez, Juan Carlos</creatorcontrib><title>Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid ( Dosidicus gigas ) Mantle Muscle</title><title>Food technology and biotechnology</title><addtitle>Food Technol Biotechnol</addtitle><description>Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid (
) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC (<1 kDa) fraction obtained from jumbo squid muscle was evaluated by Fourier transform infrared spectrometry. From its spectra, total carbohydrates, free monosaccharides, free amino acids and ammonium chloride were determined. Cryoprotectant capacity and protein cryostability conferred by LMMC were investigated by differential scanning calorimetry. Fraction partial characterization showed that the main components are free amino acids (18.84 mg/g), carbohydrates (67.1 µg/mg) such as monosaccharides (51.1 µg/mg of glucose, fucose and arabinose in total) and ammonium chloride (220.4 µg/mg). Arginine, sarcosine and taurine were the main amino acids in the fraction. LMMC, at the mass fraction present in jumbo squid muscle, lowered the water freezing point to -1.2 °C, inhibiting recrystallization at 0.66 °C. Significant myofibrillar protein stabilization by LMMC was observed after a freeze-thaw cycle compared to control (muscle after extraction of LMMC), proving the effectiveness on jumbo squid protein muscle cryo- stability. Osmolytes in LMMC fraction inhibited protein denaturation/aggregation and ice recrystallization, maintaining the muscle structure stable under freezing conditions. LMMC conferred protein cryostability even at the very low mass fraction in the muscle.</description><subject>Agglomeration</subject><subject>Amino acids</subject><subject>Ammonium</subject><subject>Ammonium chloride</subject><subject>Ammonium salts</subject><subject>Arabinose</subject><subject>Arginine</subject><subject>Biopolymer denaturation</subject><subject>Calorimetry</subject><subject>Carbohydrates</subject><subject>Cryoprotectants</subject><subject>Cryoprotectors</subject><subject>cryostability</subject><subject>Differential scanning calorimetry</subject><subject>Dosidicus gigas</subject><subject>Fish</subject><subject>Food</subject><subject>Fourier transforms</subject><subject>free amino acids</subject><subject>Freeze thaw cycles</subject><subject>Freeze-thawing</subject><subject>Freezing</subject><subject>Freezing point</subject><subject>Fucose</subject><subject>Glucose</subject><subject>Handbooks</subject><subject>Infrared spectra</subject><subject>Infrared spectroscopy</subject><subject>Melting points</subject><subject>Monosaccharides</subject><subject>Muscles</subject><subject>myofibrillar protein</subject><subject>Original Scientific Papers</subject><subject>Phase transitions</subject><subject>Protein denaturation</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Recrystallization</subject><subject>Sarcosine</subject><subject>Spectrometry</subject><subject>Spectroscopy</subject><subject>Squid</subject><subject>squid muscle</subject><subject>Studies</subject><subject>Taurine</subject><subject>Water</subject><issn>1330-9862</issn><issn>1334-2606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdUl1v0zAUjRCIfcAf4AFZ4mV7SIjt2LFfkKqOwVArkNi75dw4rask7mxnU_kH_GvcdkwM-cHWvecc34-TZe9wWeAaY_qxi03B6qLEBZYFE5V4kZ1iSquc8JK_PLzLXApOTrKzEDZlSUUt8evshGKKOanZafb7h_bR6h7N19priMbbXzpaNyLXIY0W7iFfut7A1GufL3UI6HoP2wMebFyjud-5rXfRQNRjRLOUurdxhzrvBvRtGhqHft5NtkUX6MoF21qYAlrZlQ7oEi0TpTdoOQXozZvsVaf7YN4-3ufZ7fXn2_nXfPH9y818tsiBURZzzrippWCAa0oEhVby0jAmW2Cd4A3hwnCopcFtWWvJaaOh6YhsRGVM10p6nt0cZVunN2rr7aD9Tjlt1SHg_ErtJ5IKUlo0QJMqVJxWYLgEioEZzEATSTlNWp-OWtupGUwLZoxe989En2dGu1Yrd684T7soSRK4eBTw7m4yIarBBjB9r0fjpqAIYVLitCqRoB_-g27c5Mc0qYTChHMuRZVQxRG10qkBO3Yu_QvptGaw4EbT2RSf7b3CSOoqEciRAN6F4E33VD0u1cFlKrlMsVqVWGGp9sxEev9v30-Uv7aifwCQbM-F</recordid><startdate>20190101</startdate><enddate>20190101</enddate><creator>Álvarez-Armenta, 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Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid ( Dosidicus gigas ) Mantle Muscle</title><author>Álvarez-Armenta, Andrés ; Carvajal-Millán, Elizabeth ; Pacheco-Aguilar, Ramón ; García-Sánchez, Guillermina ; Márquez-Ríos, Enrique ; Scheuren-Acevedo, Susana María ; Ramírez-Suárez, Juan Carlos</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c535t-656e7985c173283cd960e559dc5f86b268e6c79e1d07a963bacbf29b84eefd93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Agglomeration</topic><topic>Amino acids</topic><topic>Ammonium</topic><topic>Ammonium chloride</topic><topic>Ammonium salts</topic><topic>Arabinose</topic><topic>Arginine</topic><topic>Biopolymer denaturation</topic><topic>Calorimetry</topic><topic>Carbohydrates</topic><topic>Cryoprotectants</topic><topic>Cryoprotectors</topic><topic>cryostability</topic><topic>Differential scanning calorimetry</topic><topic>Dosidicus gigas</topic><topic>Fish</topic><topic>Food</topic><topic>Fourier transforms</topic><topic>free amino acids</topic><topic>Freeze thaw cycles</topic><topic>Freeze-thawing</topic><topic>Freezing</topic><topic>Freezing point</topic><topic>Fucose</topic><topic>Glucose</topic><topic>Handbooks</topic><topic>Infrared spectra</topic><topic>Infrared spectroscopy</topic><topic>Melting points</topic><topic>Monosaccharides</topic><topic>Muscles</topic><topic>myofibrillar protein</topic><topic>Original Scientific Papers</topic><topic>Phase transitions</topic><topic>Protein denaturation</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>Recrystallization</topic><topic>Sarcosine</topic><topic>Spectrometry</topic><topic>Spectroscopy</topic><topic>Squid</topic><topic>squid 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biotechnology</jtitle><addtitle>Food Technol Biotechnol</addtitle><date>2019-01-01</date><risdate>2019</risdate><volume>57</volume><issue>1</issue><spage>39</spage><epage>47</epage><pages>39-47</pages><issn>1330-9862</issn><eissn>1334-2606</eissn><abstract>Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid (
) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC (<1 kDa) fraction obtained from jumbo squid muscle was evaluated by Fourier transform infrared spectrometry. From its spectra, total carbohydrates, free monosaccharides, free amino acids and ammonium chloride were determined. Cryoprotectant capacity and protein cryostability conferred by LMMC were investigated by differential scanning calorimetry. Fraction partial characterization showed that the main components are free amino acids (18.84 mg/g), carbohydrates (67.1 µg/mg) such as monosaccharides (51.1 µg/mg of glucose, fucose and arabinose in total) and ammonium chloride (220.4 µg/mg). Arginine, sarcosine and taurine were the main amino acids in the fraction. LMMC, at the mass fraction present in jumbo squid muscle, lowered the water freezing point to -1.2 °C, inhibiting recrystallization at 0.66 °C. Significant myofibrillar protein stabilization by LMMC was observed after a freeze-thaw cycle compared to control (muscle after extraction of LMMC), proving the effectiveness on jumbo squid protein muscle cryo- stability. Osmolytes in LMMC fraction inhibited protein denaturation/aggregation and ice recrystallization, maintaining the muscle structure stable under freezing conditions. LMMC conferred protein cryostability even at the very low mass fraction in the muscle.</abstract><cop>Croatia</cop><pub>Sveuciliste U Zagrebu</pub><pmid>31316275</pmid><doi>10.17113/ftb.57.01.19.5848</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-1669-8007</orcidid><orcidid>https://orcid.org/0000-0001-5801-4593</orcidid><orcidid>https://orcid.org/0000-0001-8512-1271</orcidid><orcidid>https://orcid.org/0000-0003-4390-7457</orcidid><orcidid>https://orcid.org/0000-0003-3748-0530</orcidid><orcidid>https://orcid.org/0000-0001-8907-947X</orcidid><orcidid>https://orcid.org/0000-0001-7850-4960</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Agglomeration Amino acids Ammonium Ammonium chloride Ammonium salts Arabinose Arginine Biopolymer denaturation Calorimetry Carbohydrates Cryoprotectants Cryoprotectors cryostability Differential scanning calorimetry Dosidicus gigas Fish Food Fourier transforms free amino acids Freeze thaw cycles Freeze-thawing Freezing Freezing point Fucose Glucose Handbooks Infrared spectra Infrared spectroscopy Melting points Monosaccharides Muscles myofibrillar protein Original Scientific Papers Phase transitions Protein denaturation Protein folding Proteins Recrystallization Sarcosine Spectrometry Spectroscopy Squid squid muscle Studies Taurine Water |
| title | Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid ( Dosidicus gigas ) Mantle Muscle |
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