2022
DOI: 10.3390/polym14040751
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Characterization of Fish Gelatin Obtained from Atlantic Cod Skin Using Enzymatic Treatment

Abstract: In recent years, there has been increased interest in the production of gelatin from alternative sources, such as raw fish materials. Traditionally, gelatin is obtained using an acidic or alkaline treatment. However, these methods have some disadvantages, such as the long times for processing raw materials and the use of large amounts of water and chemicals. Furthermore, milder processing regimes are required for producing fish gelatin. Enzymes could be the solution for improving the technology of fish gelatin… Show more

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Cited by 23 publications
(13 citation statements)
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“…Antioxidants can minimize AgNP cytotoxicity [56]. Both PADM and AgNP-PADM were antioxidants, which may be because the collagen-rich PADM and AgNP-PADM hydrogels contained numerous negatively charged amino acids such as proline [23], which can combine with positively charged DPPH to scavenge oxygen free-radicals [9]. It is well known that oxygen free radicals in infected wounds will increase and aggravate local inflammation.…”
Section: Discussionmentioning
confidence: 99%
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“…Antioxidants can minimize AgNP cytotoxicity [56]. Both PADM and AgNP-PADM were antioxidants, which may be because the collagen-rich PADM and AgNP-PADM hydrogels contained numerous negatively charged amino acids such as proline [23], which can combine with positively charged DPPH to scavenge oxygen free-radicals [9]. It is well known that oxygen free radicals in infected wounds will increase and aggravate local inflammation.…”
Section: Discussionmentioning
confidence: 99%
“…Trypsin is a commercial food-grade enzyme exhibiting increased proteolytic activity and is used to break down collagen [23]. The AgNP release of the PADM and AgNP-PADM hydrogels was also measured using trypsin-containing and pure PBS.…”
Section: Release Of Agnps From Agnp-padm Hydrogelmentioning
confidence: 99%
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“…Specially, the gelatin nanostructure footprint by spectroscopy is related to the vibrational bands of the amide A (3600–2300 cm −1 ), amide I (1700–1600 cm −1 ), amide II (1500–1560 cm −1 ), and amide III (1200–1300 cm −1 ). Likewise, the analysis of the second derivative to amide band I facilitate the extraction of the rich detailed signals about the secondary structure of the gelatin ( Figure 11 , Table 6 ) [ 73 , 74 ] in good agreement with other fish [ 75 ].…”
Section: Resultsmentioning
confidence: 84%
“…The most common sources of gelatin for industrial production are porcine and bovine skins and the bones of porcine animals and cattle [ 7 ]. Globally, more than 45% of gelatin comes from porcine.…”
Section: Introductionmentioning
confidence: 99%