2021
DOI: 10.1038/s41598-021-99085-3
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Optimization of fish gelatin drying processes and characterization of its properties

Abstract: Fish skin is a raw material used for gelatin production. It can satisfy consumers with specific socio-cultural and religious needs. Different technologies have been studied for drying gelatin. Therefore, it is relevant to understand the influence of drying conditions on the final product. This study aims to optimize drying methods such as convection hot air alone and combined with infrared radiation to obtain gelatin from acoupa weakfish skin by using composite central rotational designs 22 and 23 and response… Show more

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Cited by 3 publications
(4 citation statements)
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References 42 publications
(43 reference statements)
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“…Process 1 in Figure 2 clearly shows fish gelatin with poor organoleptic properties. In this process, it is necessary to include extractive stages that deodorize and improve the sensory qualities of the final gelatin [ 16 ]. Process 2 in Figure 2 shows that the use of activated carbon in the filtering stage substantially improves the sensory aspect.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Process 1 in Figure 2 clearly shows fish gelatin with poor organoleptic properties. In this process, it is necessary to include extractive stages that deodorize and improve the sensory qualities of the final gelatin [ 16 ]. Process 2 in Figure 2 shows that the use of activated carbon in the filtering stage substantially improves the sensory aspect.…”
Section: Resultsmentioning
confidence: 99%
“…A higher yield is obtained when the extraction process is carried out with acid solutions, since the acid converts the triple helix of collagen into single chains, while the alkaline solutions transform it into double chains [ 12 ]. In addition, the method used to remove moisture is fundamental to obtaining gels with good mechanical properties, which is also key in industrial scale-up due to the high economic costs it generates [ 16 ].…”
Section: Introductionmentioning
confidence: 99%
“…The 3,410-3,448 cm −1 represents amide-A, 1,635 cm −1 represents amide-I, 1,527-1,334 cm −1 represents amide-II, and 1,242-871 cm −1 represents amide III bands. The amide-A band is owing to stretching NH vibrations, indicating gelatincoiled structure, since stretching of free NH group vibrations is generally observed at 3,400-3,440 cm −1 (22). These vibrations are beneficial for the analysis of protein secondary structure in the IR spectral region (18).…”
Section: Fourier-transform Infraredmentioning
confidence: 99%
“…These vibrations are beneficial for the analysis of protein secondary structure in the IR spectral region (18). The amide II peaks in the gelatin samples are attributed to an out-of-phase CN stretch with inplane NH deformation combination styles of the peptide groups, whereas amide III of gelatin samples is indicative of disorders in the molecules of gelatin and are possibly allied with the triplehelix structure loss (22). Kanwate et al (16) reported Amide-A at 3,294-3,273 cm −1 , Amide-B at 2,919, 2,928, and 2,919 cm −1 , Amide-I at 1,632.93, 1,634.36, and 1,631.50 cm −1 , Amide-II at 1,537, 1,529, and 1,524 cm −1 and Amide-III bands at 1,236, 1,239, and 1,236 cm −1 for freeze-dried, spray dried, and vacuum dried samples fish gelatin samples, respectively.…”
Section: Fourier-transform Infraredmentioning
confidence: 99%