Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)

European Food Research and Technology

Volumn 233, Issue 6, 2011, Pages 963-972

  Kanno, Gaku ^a   Kishimura, Hideki ^a   Yamamoto, Jun ^a   Ando, Seiichi ^b   Shimizu, Takeshi ^c   Benjakul, Soottawat ^d   Klomklao, Sappasith ^e   Nalinanon, Sitthipong ^f   Chun, Byung Soo ^g   Saeki, Hiroki ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NAYORO CITY UNIVERSITY   (Japan)

^c HOKKAIDO INDUSTRIAL TECHNOLOGY CENTER   (Japan)

^d PRINCE OF SONGKLA UNIVERSITY   (Thailand)

^e THAKSIN UNIVERSITY   (Thailand)

^f KING MONGKUT'S INSTITUTE OF TECHNOLOGY LADKRABANG   (Thailand)

^g Pukyong National University   (South Korea)

Author keywords

Arctic cod; Boreogadus saida; cDNA cloning; Cold adaptation; Primary structure; Theragra chalcogramma; Thermostability; Trypsin; Walleye pollock

Indexed keywords

ARCTIC COD; BOREOGADUS SAIDA; CDNA CLONING; COLD ADAPTATION; PRIMARY STRUCTURES; THERAGRA CHALCOGRAMMA; THERMOSTABILITY; TRYPSIN; WALLEYE POLLOCK;

ANTIGEN-ANTIBODY REACTIONS; CATALYSIS; CLONING; FISH; MAMMALS; PEPTIDES;

AMINO ACIDS;

BOREOGADUS; BOREOGADUS SAIDA; BOVINAE; THERAGRA CHALCOGRAMMA;

EID: 81355160370     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-011-1592-8     Document Type: Article

References (43)

1. Rypniewski WR, Perrakis A, Vorgias CE, Wilson KS (1994) Evolutionary divergence and conservation of trypsin. Protein Eng 7: 57-64.
2. Stroud RM, Kay LM, Dickerson RE (1974) The structure of bovine trypsin: electron density maps of the inhibited enzyme at 5 A and at 2. 7 A resolution. J Mol Biol 83: 185-208.
3. Hedstrom L, Szilagyi L, Rutter WJ (1992) Converting trypsin to chymotrypsin: the role of surface roops. Science 255: 1249-1253.
4. Hedstrom L, Perona J, Rutter WJ (1994) Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant. Biochemistry 33: 8757-8763.
5. Hedstrom L, Lin T, Fast W (1996) Hydrophobic interactions control zymogen activation in the trypsin family of serine proteases. Biochemistry 35: 4515-4523.
6. Pasternak A, Liu X, Lin T, Hedstrom L (1998) Activating a zymogen with out proteolytic processing: mutation of Lys15 and Asn194 activates trypsinogen. Biochemistry 37: 16201-16210.
7. Szabo E, Bocskei Z, Naray-Szabo G, Graf L (1999) The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the proteases. Eur J Biochem 263: 20-26.
8. Hjelmeland K, Raa J (1982) Characteristics of two trypsin type isozymes isolated from the Arctic fish capelin (Mallotus villosus). Comp Biochem Physiol 71B: 557-562.
9. Simpson BK, Haard NF (1984) Trypsin from Greenland cod, Gadus ogac. Isolation and comparative properties. Comp Biochem Physiol 79B: 613-622.
10. Asgeirsson B, Fox JW, Bjarnason JB (1989) Purification and characterization of trypsin from the poikilotherm Gadus morhua. Eur J Biochem 180: 85-94.
11. Kristjansson MM (1991) Purification and characterization of trypsin from the pyloric caeca of rainbow trout (Oncorhynchus mykiss). J Agric Food Chem 39: 1738-1742.
12. Outzen H, Berglund GI, Smalas AO, Willassen NP (1996) Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp Biochem Physiol 115B: 33-45.
13. Simpson BK, Haard NF (1987) Cold-adapted enzymes from fish. In: Knorr D (ed) Food biotechnology. Marcel Dekker, New York, pp 495-528.
14. Bjarnason JB (2000) Fish serine proteases and their pharmaceutical and cosmetic use. Patent PCT, WO 00/78332 A2, 28 Dec 2000.
15. Bjarnason JB, Benediktsson B (2001) Protein hydrolysates produced with the use of marine proteases. Patent PCT, WO 01/28353 A2, 26 Apr 2001.
16. Kishimura H, Hayashi K, Miyashita Y, Nonami Y (2005) Characteristics of two trypsin isozymes from the viscera of Japanese anchovy (Engraulis japonica). J Food Biochem 29: 459-469.
17. Kishimura H, Hayashi K, Miyashita Y, Nonami Y (2006) Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus). Food Chem 97: 65-70.
18. Kishimura H, Tokuda Y, Klomklao S, Benjakul S, Ando S (2006) Enzymatic characteristics of trypsin from the pyloric ceca of spotted mackerel (Scomber australasicus). J Food Biochem 30: 466-477.
19. Kishimura H, Tokuda Y, Klomklao S, Benjakul S, Ando S (2006) Comparative study on enzymatic characteristics of trypsins from the pyloric ceca of yellow tail (Seriola quinqueradiata) and brown hakeling (Physiculus japonicus). J Food Biochem 30: 521-534.
20. Kishimura H, Tokuda Y, Yabe M, Klomklao S, Benjakul S, Ando S (2007) Trypsins from the pyloric ceca of jacopever (Sebastes schlegeli) and elkhorn sculpin (Alcichthys alcicornis): isolation and characterization. Food Chem 100: 1490-1495.
21. Klomklao S, Benjakul S, Visessanguan W, Kishimura H, Simpson BK, Saeki H (2006) Trypsins from yellowfin tuna (Thunnus albacores) spleen: purification and characterization. Comp Biochem Physiol 144B: 47-56.
22. Klomklao S, Benjakul S, Visessanguan W, Kishimura H, Simpson BK (2006) Purification and characterization of trypsin from spleen of tongol tuna (Thunnus tonggol). J Agric Food Chem 54: 5617-5622.
23. Klomklao S, Benjakul S, Visessanguan W, Kishimura H, Simpson BK (2007) Purification and characterization of trypsins from skipjack tuna (Katsuwonus pelamis) spleen. Food Chem 100: 1580-1589.
24. Klomklao S, Benjakul S, Visessanguan W, Kishimura H, Simpson BK (2007) Trypsin from the pyloric ceca of bluefish (Pomatomus saltatrix). Comp Biochem Physiol 148B: 382-389.
25. Klomklao S, Benjakul S, Visessanguan W, Kishimura H, Simpson BK (2007) A 29 kDa protease from the digestive glands of Atlantic bonito (Sarda sarda): recovery and characterization. J Agric Food Chem 55: 4548-4553.
26. Kishimura H, Klomklao S, Benjakul S, Chun B-S (2008) Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma). Food Chem 106: 194-199.
27. Fuchise T, Kishimura H, Sekizaki H, Nonami Y, Kanno G, Klomklao S, Benjakul S, Chun B-S (2009) Purification and characteristics of cold-zone fish trypsin, Pacific cod (Gadus macrocephalus) and saffron cod (Eleginus gracilis). Food Chem 116: 611-616.
28. Kanno G, Kishimura H, Ando S, Nalinanon S, Klomklao S, Benjakul S, Chun B-S, Saeki H (2011) Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus). Eur Food Res Technol 232: 381-388.
29. Ahsan MN, Funabara D, Watabe S (2001) Molecular cloning and characterization of two isoforms of trypsinogen from anchovy pyloric ceca. Mar Biotechnol 3: 80-90.
30. Gudmundsdottir A, Gudmundsdottir E, Oskarsson S, Bjarnason JB, Eakin AK, Craik CS (1993) Isolation and characterization of cDNAs from Atlantic cod encoding two different forms of trypsinogen. Eur J Biochem 217: 1091-1097.
31. Genicot S, Rentier-Delrue F, Edwards D, Vanbeeumen J, Gerday C (1996) Trypsin and trypsinogen from Antarctic fish: molecular basis of cold adaptation. Biochim Biophys Acta 1298: 45-57.
32. Ruan G-L, Li Y, Gao Z-X, Wang H-L, Wang W-M (2010) Molecular characterization of trypsinogens and development of trypsinogen gene expression and tryptic activities in grass carp (Ctenopharyngodon idellus) and topmouth culter (Culter alburnus). Comp Biochem Physiol Part B 155: 77-85.
33. Watson MEE (1984) Compilation of published signal sequences. Nucleic Acids Res 12: 5145-5164.
34. Louvard MN, Puigserver A (1974) On bovine and porcine anionic trypsinogens. Biochim Biophys Acta 371: 177-185.
35. Huerou IL, Wicker C, Guilloteau P, Toullec R, Puigserver A (1990) Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen: structural identity within the trypsin family. Eur J Biochem 193: 767-773.
36. Krem MM, Rose T, Cera ED (1999) The C-terminal sequence encodes function in serine proteases. J Biol Chem 274: 28063-28066.
37. Leiros H-KS, Willassen NP, Smalas AO (2000) Structural comparison of psychrophilic and mesophilic trypsins: elucidating the molecular basis of cold-adaptation. Eur J Biochem 267: 1039-1049.
38. Gable D, Kasche V (1973) Autolysis of β-trypsin: influences of calcium ions and heat. Acta Chem Scand 27: 1971-1981.
39. Kanno G, Yamaguchi T, Kishimura H, Yamaha E, Saeki H (2010) Purification and characteristics of trypsin from masu salmon (Oncorhynchus masou) cultured in fresh-water. Fish Physiol Biochem 36: 637-645.
40. Walsh KA (1970) Trypsinogens and trypsins of various species. Methods Enzymol 19: 41-63.
41. Bode W, Schwager P (1975) The single calcium-binding site of crystalline β-trypsin. FEBS Lett 56: 139-143.
42. Male R, Lorens LB, Smalas AO, Torrissen KR (1995) Molecular cloning and characterization of anionic and cationic variants of trypsin from Atlantic salmon. Eur J Biochem 232: 677-685.
43. Hartley BS, Kauffman DL (1966) Corrections to the amino acid sequence of bovine chymotrypsinogen A. Biochem J 101: 229-231.