Tuna Pepsin: Characteristics and Its Use for Collagen Extraction from the Skin of Threadfin Bream (<i>Nemipterus</i> spp.)

Nalinanon, Sitthipong; Benjakul, S.; Visessanguan, Wonnop; Kishimura, Hideki

doi:10.1111/j.1750-3841.2008.00777.x

Cited by 73 publications

(67 citation statements)

References 36 publications

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“…All treatments produced similar migration bands and contained two different main bands that corresponded to α 1 and α 2 chains derived from type I collagen, which have approximate molecular weights ranging from 120 to 130 kDa (Shin, 2002). In addition, the putative higher molecular weight band of the β chain (200 kDa) was observed in all treatments (Nalinanon et al, 2008). Thus, these results indicated that type I collagen was the major collagen type in chicken skin.…”

Section: Sds-page Analysissupporting

confidence: 49%

Effects of Soaking pH and Extracting Temperature on the Physicochemical Properties of Chicken Skin Gelatin

Kim¹,

Song²,

Choi³

et al. 2012

Korean Journal for Food Science of Animal Resources

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This study was conducted to evaluate the effects of soaking pH and extraction temperature on the physicochemical properties of chicken skin gelatin. In order to extract gelatin from chicken skin, the chicken skin was soaked at various pH ranges (1-13) and was extracted at 75 and 100 o C. For the rate of weight increase, the highest value was obtained from two pH ranges (1-2 and 12-13). In addition, the rate of weight increase was affected by soaking time. The alkali treatments had greater crude protein content as well as total extraction yield compared to the acid process (p<0.05), and the increased extraction temperature resulted in a significant (p<0.05) increase of crude protein content and total extraction yield. All treatments showed α 1 and α 2 chains derived from type I collagen on SDS-PAGE. The pH value and color of gelatin gel (6.67%) were affected by soaking pH and extraction temperature. Chicken skin gelatin gel extracted at 75 o C after soaking at a pH of 2 had the highest melting point (p<0.05) and gel strength among all treatments. Although the chicken skin treated with the alkali process had a higher yield, a lower extraction temperature following the acid process would be better for obtaining superior gelatin from chicken skin.

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Section: Sds-page Analysissupporting

confidence: 49%

Effects of Soaking pH and Extracting Temperature on the Physicochemical Properties of Chicken Skin Gelatin

Kim¹,

Song²,

Choi³

et al. 2012

Korean Journal for Food Science of Animal Resources

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“…Fish skin can be used as an alternative source for collagen since mammalian collagens are associated with several problems such as the outbreak of mad cow disease and the constraint for some religions, mainly Islam and Judaism (Nalinanon et al 2008). Therefore, skin collagens from several fish species such as bigeye snapper (Kittiphattanabawon et al 2005;Nalinanon et al 2007), black drum (Ogawa et al 2003), brown stripe red snapper (Jongjareonrak et al 2005), carp (Duan et al 2009), channel catfish ), Nile perch (Muyonga et al 2004), oscillate puffer fish (Nagai et al 2002), sheephead seabream (Ogawa et al 2003), threadfin bream (Nalinanon et al 2008) and yellowfin tuna (Woo et al 2008) have been extracted and characterized. Although there are many reports about collagen from skin of marine organisms, there are few studies of fish scales like the studies of Kimura et al (1991) and those of Shirai (Nomura et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of collagen from fish waste material- skin, scales and fins of Catla catla and Cirrhinus mrigala

Mahboob

2014

J Food Sci Technol

117

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The collagen of skin, scales and fins of Catla catla and Cirrhinus mrigala were isolated and characterised. Nine fishes of each fish species of three weight groups were collected from a commercial fish farm. Collagen characterisation using SDS-PAGE revealed the molecular weights (kDa) of the C. catla skin, scales, and fins which ranged from 120 to 210, 70 to 201, and 68 to 137 kDa, respectively. The size of the collagen of C. mrigala skin, scales and fins ranged from 114 to 201, 77 to 210, and 70 to 147 kDa, respectively. Glycine and alanine were the most abundant amino acid, whereas tryptophan was totally absent in all selected tissues. Thus, significant variation exists in type of collagen and amino acid profile within the weight groups of the two fish species. The imino acid (proline and hydroxyproline) contents estimated in C. catla and C. mrigala skin (161-165 and 160-168), scales (155-159 and 152-161) and fins (162-171 and (152-155) residues/1,000 residues, respectively. The proximate analysis was also performed for skin, scales and fins. The maximum protein content of the skin was determined as 26.10 % and 22.90 % in the C. catla and C. mrigala, respectively, from the W 3 weight group. The scales of the W 3 weight group exhibited maximum protein contents of 25.90 and 21.77 % for C. catla and C. mrigala, respectively. The maximum protein contents (19.04 % and 18.12 %) were recorded for C. catla and C. mrigala, respectively in the fins.

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“…The main inhibitors and activators of pepsin are shown in table 2. The enzymatic activity of pepsin is almost completely inhibited by pepstatin A (aspartic proteinase competitive inhibitor that binds strongly to residues of the active site of the enzyme) and partially inhibited by phenyl methyl sulfonyl fluoride (PMSF, serinoproteinase inhibitor), L-3-carboxytrans-2, 3-epoxy-propionyl-L-leucyl-4-guanidino-butylamide (E-64), cysteine, molybdate and EDTA (Ethylenediamine tetra acetic acid, specific for metalloproteases) (DIAZ-LOPEZ et al, 1998;CASTILLO-YAÑEZ et al, 2004;TANJI et al, 2007;BOUGATEF et al, 2008;KLOMKLAO et al, 2007;NALINANON et al, 2008;NALINANON et al, 2010;WU et al, 2009;CAO et al, 2011;ZHAO et al, 2011). In contrast, the activity increases in the presence of divalent cations such as CaCl 2 , MgCl 2 and CoCl 2 (El-BELTAGY et al, 2004;KLOMKLAO et al, 2007).…”

Section: Factors Affecting the Activity (Ph Temperature Activators mentioning

confidence: 99%

“…The enzyme is also utilized in the production of fish silage, in the use of byproducts of fish processing industry and in the animal feed industry for increase protein digestibility. It is considered a promising protease with extensive industrial application of efficient effect if effective techniques for their recovery and purification can be developed (KAGEYAMA, 2002;KLOMKLAO et al, 2007;NALINANON et al, 2008;EISENMENGER & REYES-DE-CORCUERA, 2009;ZHAO et al, 2011;ZENG et al, 2012).…”

Section: Biotechnological Applicationsmentioning

confidence: 99%

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Fish pepsin: basic characteristics, extraction, determination and biotechnological applications

2015

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Enzyme technology has been employed in various segments of the industry, food production and consumer goods. Fish viscera are potential sources of proteins with enzymatic properties appreciable in this market. Among them, pepsin (EC 3.4.23.x) deserves special attention. The active enzyme has at least five isoforms which are precursor groups of pepsins type: A, B, and F, gastricsin and chymosin. Their zymogen (pepsinogen) is activated by autocatalysis at acidic pH in stomach. Hemoglobin is their specific substrate. Features like optimal pH and temperature vary according to species and even within the same species may be found different values. The molecular weight also varies according to species and is generally between 25 and 35 kDa. The protocols for extraction and determination of pepsin fish follow a line of standardization, varying concentrations of analysis. These data are basic steps to detect the presence of the enzyme targeting a future purification process for its effective biotechnological applications. KEYWORDS:Digestive; Enzyme; Fish; Pepsin; Biotechnology. PEPSINA DE PEIXES: CARACTERÍSTICAS BÁSICAS, EXTRAÇÃO, DETERMINAÇÃO E APLICAÇÕES BIOTECNOLÓGICAS RESUMOTecnologia enzimática vem sendo empregada em diversos segmentos da indústria, da produção de alimentos e bens de consumo. Vísceras de peixes são potenciais fontes de proteínas com propriedades enzimáticas apreciáveis neste mercado. Entre eles, a pepsina (EC 3.4.23.x) merece atenção especial. A enzima ativa tem, pelo menos, cinco isoformas, sendo elas precursoras do tipo pepsinas: A, B e F, gastricsina e quimosina. O zimogênio (pepsinogênio) é ativado por autocatálise em pH ácido do estômago que vem do ácido clorídrico. A hemoglobina é seu substrato específico. Características como temperatura e pH ótimos variam de acordo com as espécies e até mesmo dentro da mesma espécie podem ser encontrados valores diferentes. O peso molecular varia também de acordo com a espécie e situa-se geralmente, entre 25 e 35 kDa. Os protocolos de extração e de determinação de pepsina de peixe seguem uma linha de normalização, com várias concentrações de análise. Estes dados são passos básicos para detectar a presença da enzima destinada a um futuro processo de purificação para aplicações biotecnológicas eficazes.

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Tuna Pepsin: Characteristics and Its Use for Collagen Extraction from the Skin of Threadfin Bream (Nemipterus spp.)

Cited by 73 publications

References 36 publications

Effects of Soaking pH and Extracting Temperature on the Physicochemical Properties of Chicken Skin Gelatin

Effects of Soaking pH and Extracting Temperature on the Physicochemical Properties of Chicken Skin Gelatin

Isolation and characterization of collagen from fish waste material- skin, scales and fins of Catla catla and Cirrhinus mrigala

Fish pepsin: basic characteristics, extraction, determination and biotechnological applications

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