Chemical composition and characteristics of skin gelatin from grey triggerfish (Balistes capriscus)

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“…As shown in Table 2, the gel strength after overnight maturation at 6 o C was higher (P<0.05) for Volga pikeperch. Both values were higher than those of gelatins from many fish species previously reported although differences in method may have a major impact: red tilapia (128 g), black tilapia (181 g) (Jamilah & Harvinder, 2002), cod (71 (Cheow et al, 2007), cuttlefish (181 g) , grey triggerfish (168 g) (Jellouli et al, 2011), rohu (124 g), tuna (177 g) (Shyni et al, 2014), tuna fin (126 g) (Aewsiri, Benjakul, Visessanguan, & Tanaka, 2008) and common carp (185 g) (Mostafa et al, 2015). However, both gel strengths were lower than from shark skins (206 g) (Shyni et al, 2014), rohu skins (258 g) and mrigal skins (343 g) (Madhamuthanalli & Bangalore, 2014).…”

“…Glycine, the most abundant amino acid found in gelatin, accounted for ~23% of the total amino acids, which suggests potential non-gelatin impurities. The percentage of glycine was lower than those of gelatins from kumakuma (25%) (Silva et al, 2017), grey triggerfish (29%) (Jellouli et al, 2011) and carp (33%) (Duan, Zhang, Xing, Konno, & Xu, 2011), but higher than those of gelatins from cornet fish (21%) (Nazeer & Deepthi, 2013), lizardfish scale (18%) (Wangtueai & Noomhorm, 2009) and jellyfish (19%) (Cho, Ahn, Koo, & Kim, 2014). The proportion of essential amino acids of two gelatins were similar to those of cornet fish gelatin (22%) (Nazeer & Deepthi, 2013), kumakuma gelatin (25%) (Silva et al, 2017), and higher than those of gelatins from carp (13%) (Duan et al, 2011), cuttlefish (14%) , grey triggerfish (17%), cobia (13%) and croaker (15%) (Silva et al, 2014).…”

“…The higher content of essential amino acids was mainly due to the higher content of valine while the others were similar to the values of other fish. The valine content of gelatins were much higher than those from grey triggerfish (3%) (Jellouli et al, 2011), cuttlefish (2%) , carp (2%) (Duan et al, 2011), cobia (2%), croaker (2%) (Silva et al, 2014) and kumakuma (2%) (Silva et al, 2017). It is known that the thermal stability of collagen is affected by the content of the imino acids, and the proportion of these amino acids is related to the habitat temperature of the fish (Kimura, Zhu, Matsui, Shijoh, & Takamizawa, 1988).…”

Extraction and Characterization of Gelatin from Bovine Lung

“…The CBG standard had the highest foam stabilities at 0.5 and 2% gelatin concentrations and EAI values at the 1 and 2% gelatin concentrations (Table 4). Jellouli et al (2011) reported that the higher foaming capacity of grey trigger fish gelatin compared to that of bovine gelatin was due to the increased content of hydrophobic amino acid contents (alanine, valine, isoleucine, leucine, proline, methionine, phenylalanine and tyrosine) in trigger fish gelatin. Results of the present study do not agree with Jellouli et al (2011) as there was no clear pattern of differences in the hydrophobic amino acids between heat and pepsin extracted gelatins (Table 3).…”

“…Jellouli et al (2011) reported that the higher foaming capacity of grey trigger fish gelatin compared to that of bovine gelatin was due to the increased content of hydrophobic amino acid contents (alanine, valine, isoleucine, leucine, proline, methionine, phenylalanine and tyrosine) in trigger fish gelatin. Results of the present study do not agree with Jellouli et al (2011) as there was no clear pattern of differences in the hydrophobic amino acids between heat and pepsin extracted gelatins (Table 3). Foams with high concentrations of proteins have increased foaming densities and stabilities (Zayas, 1997) and emulsifying ability is governed by protein peptide size, with small peptides being more soluble and having a greater ability to form a film around an oil droplet than large peptides (Kittiphattanabawon et al, 2012).…”