Characterization of Bacillus kaustophilus leucine aminopeptidase immobilized in Ca-alginate/k-carrageenan beads

Biochemical Engineering Journal

Volumn 39, Issue 2, 2008, Pages 376-382

  Chi, Meng Chun ^a   Lyu, Rui Cin ^b   Lin, Long Liu ^b   Huang, Hsien Bin ^a  

^a NATIONAL CHUNG CHENG UNIVERSITY   (Taiwan)

^b NATIONAL CHIAYI UNIVERSITY   (Taiwan)

Author keywords

Alginate; Bacillus kaustophilus; Immobilization; k Carrageenan; Leucine aminopeptidase; Stability

Indexed keywords

ALGINATE; CALCIUM; ENZYME ACTIVITY; HYDROGELS; OXIDATION;

BACILLUS KAUSTOPHILUS; LEUCINE AMINOPEPTIDASE;

PLANTS (BOTANY);

CALCIUM ALGINATE; CARRAGEENAN; CYTOSOL AMINOPEPTIDASE;

ALKALINITY; ARTICLE; BACILLUS; BACILLUS KAUSTOPHILUS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME IMMOBILIZATION; HYDROGEL; INCUBATION TIME; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE; THERMOSTABILITY;

GEOBACILLUS KAUSTOPHILUS;

EID: 40049101302     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2007.10.008     Document Type: Article

References (50)

1. Binkley F., and Torres C. Spectrophotometric assay of peptidase activity. Arch. Biochem. Biophys. 86 (1960) 201-203
2. Lee H.J., LeRue J.N., and Wilson I.B. A simple spectrophotometric assay for amino acyl arylamidases (naphthylamidases, aminopeptidases). Anal. Biochem. 41 (1971) 397-401
3. Tuppy H., Wiesbauer U., and Wintersberger E. Amino acid-p-nitroanilide as a substrate for aminopeptidases and other proteolytic enzymes. Hoppe-Seyler's Z. Physiol. Chem. 329 (1962) 278-288
4. Saifuku K., Sekine T., Namihisa T., Takahashi T., and Kanoaka Y. A novel fluorometric ultramicro determination of serum leucine aminopeptidase using a coumarine derivative. Clin. Chim. Acta 84 (1978) 85-91
5. Terenius L., Sandin J., and Sakurada T. Nociceptin/orphanin FQ metabolism and bioactive metabolites. Peptides 21 (2000) 919-922
6. Goldberg A.L., Cascio P., Saric T., and Rock K.L. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol. Immunol. 39 (2002) 147-164
7. Toldrá F., Aristoy A.C., and Flores M. Contribution of muscle aminopeptidases to flavor development in dry-cured ham. Food Res. Int. 33 (2000) 181-185
8. Raksakulthai R., and Haard N.F. Exopeptidases and their application to reduce bitterness in food: a review. Crit. Rev. Food Sci. Nutr. 43 (2003) 401-445
9. FitzGerald R.J., and O'Cuinn G. Enzymatic debittering of food hydrolysates. Biotechnol. Adv. 24 (2006) 234-237
10. Kamphuis J., Meijer E.M., Boesten W.H.J., Broxterman Q.B., Kaptein B., Hermes H.F.M., and Schoemaker H.E. Production of natural and synthetic l- and d-amino acids by aminopeptidases and amino amidases. In: Rozzell J.D., and Wagner F. (Eds). Biocatalytic Production of Amino Acids and Derivatives (1992), Wiley, New York 178-206
11. Tischer W., and Kasche V. Immobilized enzymes: crystals or carriers?. Trends Biotechnol. 17 (1999) 326-335
12. Roy I., Sharma S., and Gupta M.N. Smart biocatalysts: design and applications. Adv. Biochem. Eng. Biotechnol. 86 (2004) 159-189
13. Heng P.W.S., and Chan L.W. Effect of aldehydes and methods of cross-linking on properties of calcium alginate microspheres prepared by emulsification. Biometerials 23 (2002) 1319-1326
14. Heng P.W.S., Chan L.W., and Jin Y. Cross-linking mechanisms of calcium and zinc in production of alginate microspheres. Int. J. Pharm. 242 (2002) 255-258
15. Heng P.W.S., Chan L.W., and Lee H.Y. Production of alginate microspheres by internal gelation using an emulsification method. Int. J. Pharm. 242 (2002) 259-262
16. Smidsrød O., and Skjäk-Bræk G. Alginate as immobilization matrix for cells. Trends Biotechnol. 8 (1990) 71-78
17. Sarder M., Roy I., and Gupta M.N. A smart bioconjugate of alginate and pectinase with unusual biological activity toward chitosan. Biotechnol. Prog. 19 (2003) 1654-1658
18. Zhu H., Srivastava R., Brown J.Q., and McShane M.J. Combined physical and chemical immobilization of glucose oxidase in alginate microspheres improves stability of encapsulation and activity. Bioconj. Chem. 16 (2005) 1451-1458
19. Şahin F., Demirel G., and Tümtürk H. A novel matrix for the immobilization of acetylcholinesterase. Int. J. Biol. Macromol. 37 (2005) 148-153
20. Mondal K., Mehta P., Mehta B.R., Varandani D., and Gupta M.N. A bioconjugate of Pseudomonas cepacia lipase with alginate with enhanced catalytic efficiency. Biochim. Biophys. Acta 1764 (2006) 1080-1086
21. Mittal A., Khurana S., Singh H., and Kamboj R.C. Characterization of dipeptidylpeptidase IV (DPP IV) immobilized in Ca alginate beads. Enzyme Microb. Technol. 37 (2005) 318-323
22. Lin L.L., Hsu W.H., Wu C.P., Chi M.C., Chou W.M., and Hu H.Y. A thermostable leucine aminopeptidase from Bacillus kaustophilus CCRC 11223. Extremophiles 8 (2004) 79-87
23. Chi M.C., Chou W.M., Wang C.H., Chen W., Hsu W.H., and Lin L.L. Generating oxidation-resistant variants of Bacillus kaustophilus leucine aminopeptidase by substitution of the critical methionine residues with leucine. Anotnie van Leeuwenhoek 86 (2004) 355-362
24. Chi M.C., Chou W.M., Hsu W.H., and Lin L.L. Identification of amino acid residues essential for catalytic reaction of Bacillus kaustophilus leucine amniopeptidase. Biosci. Biotechnol. Biochem. 68 (2004) 1794-1797
25. Chi M.C., Huang H.B., Liu J.S., Wang W.C., Liang W.C., and Lin L.L. Residues threonine 346 and leucine 352 are critical for the proper function of Bacillus kaustophilus leucine aminopeptidase. FEMS Microbiol. Lett. 260 (2006) 156-161
26. Burley S.K., David P.R., Sweet R.M., Taylor A., and Lipscomb W.N. Structure determination of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 224 (1992) 113-140
27. Sträter N., Sun L., Kantrowitz E.R., and Lipscomb W.N. A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by zinc leucine aminopeptidase. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 11151-11155
28. Sträter N., and Lipscomb W.N. Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of l-leucinal, a gem-diolate transition state analogue, by X-ray crystallography. Biochemistry 34 (1995) 14792-14800
29. Huang H.B., Chi M.C., Hsu W.H., Liang W.C., and Lin L.L. Construction and one-step purification of Bacillus kaustophilus leucine aminopeptidase fused to the starch-binding domain of Bacillus sp. strain TS-23 α-amylase. Bioprocess Biosyst. Eng. 27 (2005) 389-398
30. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
31. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227 (1977) 680-685
32. Farag A.M., and Hassan M.A. Purification, characterization, and immobilization of a keratinase from Aspergillus oryzae. Enzyme Microb. Technol. 34 (2004) 85-93
33. Doumèche B., Heinemann M., Büchs J., Hartmeier W., and Ansorge-Schumacher M.B. Enzymatic catalysis of gel-stabilized two-phase systems: improvement of the solvent phase. J. Mol. Catal. B Enzym. 18 (2002) 19-27
34. Lipotov S.Y. Polymer blends and interpenetrating polymer networks at the interface with solids. Prog. Polym. Sci. 27 (2002) 1721-1801
35. Bajpai A.K., Bajpai P., and Shukla S. Water sorption through a semi-interpenetrating polymer network (IPN) with hydrophilic and hydrophobic chains. React. Funct. Polym. 50 (2001) 9-21
36. Kara F., Demirel G., and Tümtürk H. Immobilization of urease by using chitosan-alginate and poly (acrylamide-co-acrylic acid)/k-carrageenan supports. Bioprocess Biosyst. Eng. 29 (2006) 207-211
37. Tümtürk H., Karaca N., Demirel G., and Şahin F. Preparation and application of poly (N,N-dimethylacrylamide-co-acrylamide) and poly (N-isopropylacrylamide-co-acrylamide)/k-carrageenan hydrogels for immobilization of lipase. Int. J. Biol. Macromol. 40 (2007) 281-285
38. Vaillant F., Millan A., Millan P., Dornier M., Decloux M., and Reynes M. Co-immobilized pectinlyase and endocellulase on chitin and nylon supports. Process Biochem. 35 (2000) 989-996
39. Yahşi A., Şahin F., Demirel G., and Tümtürk H. Binary immobilization of tyrosinase by using alginate gel beads and poly(acrylamide-co-acrylic acid) hydrogels. Int. J. Biol. Macromol. 36 (2005) 253-258
40. Puri M., Marwaha S.S., and Kothari R.M. Studies on the applicability of alginate-entrapped naringinase for the debittering of kinnow juice. Enzyme Microb. Technol. 18 (1996) 281-285
41. Palmieri G., Giardina P., Desiderio B., Morzullo L., Giamberini M., and Sannia G. A new enzyme immobilization procedure using copper alginate gel: application to a fungal phenol oxidase. Enzyme Microb. Technol. 16 (1994) 151-158
42. Cao L. Immobilized enzymes: science or art?. Curr. Opin. Chem. Biol. 9 (2005) 217-226
43. Munjal N., and Sawhney S.K. Stability and properties of mushroom tyrosinase entrapped in alginate, polyacrylamide and gelatin gels. Enzyme Microb. Technol. 30 (2002) 613-619
44. Blandino A., Macías M., and Cantero D. Glucose oxidase release from calcium alginate gel capsules. Enzyme Microb. Technol. 27 (2000) 319-324
45. Leckband D., and Langer R. An approach for the stable immobilization of proteins. Biotechnol. Bioeng. 37 (1991) 227-237
46. Longo M.A., Novella I.S., Garcia L.A., and Diaz M. Diffusion of proteases in calcium alginate beads. Enzyme Microb. Technol. 14 (1992) 586-590
47. Arica M.Y., and Bayramoǧlu G. Reversible immobilization of tyrosinase onto polyethyleneimine-grafted and Cu(II) chelated poly(HEMA-co-GMA) reactive membranes. J. Mol. Catal. B Enzym. 27 (2004) 255-265
48. Stadtman E.R. Oxidation of proteins by mixed-function oxidation systems: implication in protein turnover, aging and neutrophil. Trends Biochem. Sci. 11 (1986) 11-12
49. Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62 (1993) 797-821
50. Ciolino H.P., and Levine R.L. Modification of proteins in endothelial cell death during oxidative stress. Free Radic. Biol. Med. 22 (1997) 1277-1282