Purification and characterization of chymotrypsins from the hepatopancreas of crucian carp (Carassius auratus)

Yang, Feng; Su, Wen‐Jin; Lu, Bao-Ju; Wu, Tao; Sun, Le-Chang; Hara, Kenji; Cao, Min‐Jie

doi:10.1016/j.foodchem.2009.03.035

Cited by 31 publications

(55 citation statements)

References 22 publications

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“…Chymotrypsin exists in three inactive forms (chymotrypsinogens A, B and C) in the zymogen granules (dense, membrane-bound bodies that are derived from the Golgi body of cells) of the pancreas (Smith et al, 1951;Geiger, 1985;Raae, 1995;LethLarsen et al, 1996). The three types of chymotrypsin (A, B, C) have been found in mammals but only two types of chymotrypsin (A and B) have been found in fish (Yang et al, 2009). As a one of the main digestion proteases, chymotrypsin has been widely reported in the gut of a variety of fish including: discus (Symphysodon sp.…”

Section: Function and Strycture Of Chymotrypsinmentioning

confidence: 99%

“…Fish chymotrypsin usually has two different forms: cationic (chymotrypsin B) and anionic (chymotrypsin A) (Yang et al, 2009). The isoelectric points of fish chymotrypsinogens A and B are at the pHs of 9.1 and 5.2, respectively.…”

Section: Function and Strycture Of Chymotrypsinmentioning

confidence: 99%

“…The amino acid sequences of chymotrypsins A and B are very similar with only minor differences and the activated enzymes contain three polypeptide chains. The two isoforms of chymotrypsin (A and B) have been found in and extracted from rainbow trout (Kristjansson and Nielson, 1992), grass carp (Fong et al, 1998), Altantic cod (Ásgeirsson et al, 1993), anchovy (Heu et al, 1995), Monterey sardine (Castillo-Yañez et al 2006) and crucian carp (Yang et al, 2009).…”

Section: Function and Strycture Of Chymotrypsinmentioning

confidence: 99%

“…Similar observations were reported by other researchers (Fersht and Requena, 1971;Lucas et al, 1973;Leslie and Wang, 1968). (Castillo-Yañez et al, 2009;Yang et al, 2009) Residual enzyme activity (%) Inhibitors: Synthetic and natural inhibitors can decrease the ability of chymotrypsin to hydrolyze proteins or peptides by forming enzyme-inhibitor structures (Guha and Sinha, 1984;Makkar et al, 2007). Natural chymotrypsin inhibitors are found in plants such as phaseolus lunatus, black gram, macrotyloma axillare, solanum tuberosum, pigeon pea, chick pea, erythrina caffra and patato (Makkar et al, 2007) or animal sources such as egg whites (Guha and Sinha, 1984).…”

Section: Mechanism Of Catalyzed Hydrolysismentioning

confidence: 99%

“…Synthetic chymotrypsin inhibitors such as N-Toluenesulfonyle-Phenylalanine Chloromethyl Ketone (TPCK), N-carbobenzoxy-(Gly)2-Phenylalanine Chloromethyl Ketone (ZGGPCK), N-carbobenzoxy -L-phenylalanine Chloromethyl Ketone (ZPCK) and chymostatin are chymotrypsin specific and can dramatically inhibit the catalyzing power of chymotrypsin (Heu et al, 1995;Sabapathy and Teo., 1995;Tokumoto et al, 1999;Santigosa et al, 2008).The effects of inhibitors on the chymotrypsin activity are shown in Table 1. Serine proteinase inhibitors such as Phenylmethanesulfonyl Fluoride (PMSF) and 4-(2-Aminoethyl)-benzenesulfonyl fluoreide (Pefabloc SC) effectively inhibit the activity of chymotrypsin (Elert et al, 2004;Yang et al, 2009) while asparatic proteinase inhibitors such as pepstatin and the metalloproteinase inhibitor EDTA have slight influences on chymotrypsin (Yang et al, 2009;Heu et al, 1995;Castillo-Yañez et al, 2006 (Castillo-Yañez et al, 2006;Yang et al, 2009).…”

Section: Mechanism Of Catalyzed Hydrolysismentioning

confidence: 99%

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Extraction, Purification and Characterization of Fish Chymotrypsin: A Review

K.¹

2011

American Journal of Biochemistry and Biotechnology

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Problem statement: Solid fish waste is generated from the unwanted parts of fish including heads, tails, fins, frames, offal (guts, kidney and liver) and skin. It accounts for up to 80% of material from production of surimi, 66% from production of fillet and 27% from production of headed and gutted fish. Currently, fish wastes are disposed off in land-based waste disposal systems or at sea generating toxic byproducts during the decomposition process. However, fish processing waste can be used to produce commercially valuable by-products, such as chymotrypsin. Approach: A comperehensive review of the literature on the extraction, purification and characeterization of fish chymotrypsin was performed. Results: Chymotrypsin is an endopeptidase secreted by the pancreatic tissues of vertebrates and invertebrates. It has 3 different structures (chymotrypsin A, B and C) varying slightly in solubility, electrophoretic mobility, isoelectric point and cleavage specificity. Only chymotrypsin A and B are found in fish. Compared with mammal chymotrypsin, fish chymotrypsins have similar amino acid composition and molecular weights. Fish chymotrypsins have higher specific activity, especially those from cold-water fish, and low pH and temperature tolerance. The factors affecting the concentration and activity of chymotrypsin in fish are water temperature, fish species, fish age, fish weight and starvation. Chymotrypsin has application in various industries including the food industry, leather production industry chemical industry and medical industry. Conclusion: Extraction techniques for chymotrypsin include: ultra-filtration, ammonium sulphate fractionation precipitation or water-in-oil microemulsions. Purification can be carried out using recrystallization and gel-filtration, ion-exchange and hydrophobic interaction chromatography. Further studies should focus on the optimization of purifiying chymotrypsin from fish processing wastes.

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Section: Function and Strycture Of Chymotrypsinmentioning

confidence: 99%

Section: Function and Strycture Of Chymotrypsinmentioning

confidence: 99%