Influence of collagen and some proteins on gel properties of jellyfish gelatin

Autor: Sittiruk Roytrakul, Sawanya Charoenlappanit, Savitri Vatanyoopaisarn, Artima Lueyot, Pisit Wongsa-ngasri, Benjawan Thumthanaruk, Vilai Rungsardthong, Benjamaporn Wonganu, Pokkwan Hutangura
Jazyk: angličtina
Rok vydání: 2021
Předmět:
0106 biological sciences
Proteomics
Jellyfish
Scyphozoa
Raw Materials
Marine and Aquatic Sciences
01 natural sciences
Gelatin
Biochemistry
Physical Chemistry
chemistry.chemical_compound
Animal Products
Materials Physics
Tandem Mass Spectrometry
Marine Fish
Materials
Multidisciplinary
biology
Chemistry
Viscosity
Organic Compounds
Physics
Bovine gelatin
Eukaryota
Agriculture
04 agricultural and veterinary sciences
Melting
Condensed Matter Physics
040401 food science
Physical Sciences
Vertebrates
Medicine
Thickening
Collagen
Phase Transitions
Research Article
food.ingredient
Fat content
Science
Materials Science
Hydrochloric acid
Marine Biology
Cnidaria
0404 agricultural biotechnology
food
010608 biotechnology
biology.animal
Animals
Chromatography
Extraction (chemistry)
Organic Chemistry
Organisms
Chemical Compounds
Biology and Life Sciences
Proteins
Invertebrates
Amides
Hot water extraction
Fish
Chemical Properties
Earth Sciences
Zoology
Collagens
Gels
Chromatography
Liquid
Zdroj: PLoS ONE
PLoS ONE, Vol 16, Iss 6, p e0253254 (2021)
ISSN: 1932-6203
Popis: Marine gelatin is one of the food proteins used in food and non-food products, offering desirable functionalities such as gelling, thickening, and binding. Jellyfish has been chosen for this gelatin research, in view of the benefits of its main collagen protein and lower fat content, which may reduce the amounts of chemicals used in the preparative steps of gelatin production. To date, the lack of identified proteins in gelatin has limited the understanding of differentiating intrinsic factors quantitatively and qualitatively affecting gel properties. No comparison has been made between marine gelatin of fish and that of jellyfish, regarding protein type and distribution differences. Therefore, the study aimed at characterizing jellyfish gelatin extracted from by-products, that are i.e., pieces that have broken off during the grading and cleaning step of salted jellyfish processing. Different pretreatment by hydrochloric acid (HCl) concentrations (0.1 and 0.2 M) and hot water extraction time (12 and 24 h) were studied as factors in jellyfish gelatin extraction. The resultant jellyfish gelatin with the highest gel strength (JFG1), as well as two commercial gelatins of fish gelatin (FG) and bovine gelatin (BG), were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). The results show that the jellyfish gelatin (JFG1) extracted with 0.1 M HCl at 60°C for 12 h delivered a maximum gel strength of 323.74 g, which is lower than for FG and BG, exhibiting 640.65 and 540.06 g, respectively. The gelling and melting temperatures of JFG1 were 7.1°C and 20.5°C, displaying a cold set gel and unstable gel at room temperature, whereas the gelling and melting temperatures of FG and BG were 17.4°C, 21.3°C, and 27.5°C, 32.7°C, respectively. Proteomic analysis shows that 29 proteins, of which 10 are types of collagen proteins and 19 are non-collagen proteins, are common to all BG, FG, and JFG1, and that JFG1 is missing 3 other collagen proteins (collagen alpha-2 (XI chain), collagen alpha-2 (I chain), and collagen alpha-2 (IV chain), that are important to gel networks. Thus, the lack of these 3 collagen types influences the inferior gel properties of jellyfish gelatin.
Databáze: OpenAIRE
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