Effect of ultrasound on the activity and conformation of α-amylase, papain and pepsin

Ultrasonics Sonochemistry

Volumn 21, Issue 3, 2014, Pages 930-936

  Yu, Zhi Long ^a   Zeng, Wei Cai ^a   Zhang, Wen Hua ^a   Liao, Xue Pin ^a   Shi, Bi ^a  

^a SICHUAN UNIVERSITY   (China)

Author keywords

Conformation; Enzyme activity; Papain; Pepsin; Ultrasound; Amylase

Indexed keywords

AMINO ACIDS; CIRCULAR DICHROISM SPECTROSCOPY; CONFORMATIONS; DICHROISM; ENZYME ACTIVITY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; PAPAIN; ULTRASONIC EQUIPMENT; ULTRASONICS;

CONFORMATIONAL CHANGE; FOURIER TRANSFORM INFRA REDS; ORIGINAL STRUCTURES; PEPSIN; SECONDARY AND TERTIARY STRUCTURES; STRUCTURAL COMPONENT; TRYPTOPHAN FLUORESCENCE INTENSITY; ULTRASONIC TREATMENTS;

AMYLASES;

AMYLASE; PAPAIN; PEPSIN A; TRYPTOPHAN;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; FLUORESCENCE SPECTROSCOPY; INFRARED SPECTROSCOPY; IRRADIATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; ULTRASOUND;

CONFORMATION; ENZYME ACTIVITY; PAPAIN; PEPSIN; ULTRASOUND; Α-AMYLASE;

ALPHA-AMYLASES; ANIMALS; BACILLUS; CARICA; HYDROLASES; PAPAIN; PEPSIN A; PROTEIN CONFORMATION; SWINE; ULTRASONICS;

EID: 84895072413     PISSN: 13504177     EISSN: 18732828     Source Type: Journal    
DOI: 10.1016/j.ultsonch.2013.11.002     Document Type: Article

References (42)

1. J. Chandrapala, C. Oliver, S. Kentish, and M. Ashokkumar Ultrasonics in food processing Ultrason. Sonochem. 19 2012 975 983
2. F. Chemat, Z. Huma, and M.K. Khan Applications of ultrasound in food technology: processing, preservation and extraction Ultrason. Sonochem. 18 2011 813 835
3. H. Feng, W. Yang, and T. Hielscher Power ultrasound Food Sci. Technol. Int. 14 2008 433 436
4. A. DemÑ-rdöven, and T. Baysal The use of ultrasound and combined technologies in food preservation Food Rev. Int. 25 2009 1 11
5. C.P. O'Donnell, B.K. Tiwari, P. Bourke, and P.J. Cullen Effect of ultrasonic processing on food enzymes of industrial importance Trends Food Sci. Tech. 21 2010 358 367
6. Z.B. Wang, X.M. Lin, P.P. Li, J. Zhang, S.Q. Wang, and H.L. Ma Effects of low intensity ultrasound on cellulase pretreatment Bioresource Technol. 117 2012 222 227
7. R.C. Minussi, G.M. Pastore, and N. Durán Potential applications of laccase in the food industry Trends Food Sci. Tech. 13 2002 205 216
8. F. Shahidi, and Y.J. Kamil Enzymes from fish and aquatic invertebrates and their application in the food industry Trends Food Sci. Tech. 12 2001 435 464
9. R. Gupta, P. Gigras, H. Mohapatra, V.K. Goswami, and B. Chauhan Microbial α-amylases: a biotechnological perspective Process Biochem. 38 2003 1599 1616
10. E. Amri, and F. Mamboya Papain, a plant enzyme of biological importance. a review Am. J. Biochem. Biotechnol. 8 2012 99 104
11. I. Arcan, and A. Yemenicioǧlu Effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea proteins Food Res. Int. 43 2010 140 147
12. C.H. Han, J.C. Liu, S.U. Fang, and W.C. Hou Antioxidant activities of the synthesized thiol-contained peptides derived from computer-aided pepsin hydrolysis of yam tuber storage protein, dioscorin Food Chem. 138 2013 923 930
13. Z.L. Yu, W.C. Zeng, and X.L. Lu Influence of ultrasound to the activity of tyrosinase Ultrason. Sonochem. 20 2013 805 809
14. R.F. Contamine, A.M. Wilhelm, J. Berlan, and H. Delmas Power measurement in sonochemistry Ultrason. Sonochem. 2 1995 S43 S47
15. G. Böhm, R. Muhr, and R. Jaenicke Quantitative analysis of protein far UV circular dichroism spectra by neural networks Protein Eng. 5 1992 191 195
16. G.L. Miller Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal. Chem. 31 1959 426 428
17. C. Cupp-Enyard Sigma's non-specific protease activity assay - casein as a substrate J. Vis. Exp. 19 2008 e899
18. B. Ranjbar, and P. Gill Circular dichroism techniques: biomolecular and nanostructural analyses - a review Chem. Biol. Drug Des. 74 2009 101 120
19. N.J. Greenfield Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 1 2006 2876 2890
20. B.A. Wallace, and R.W. Janes Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics Curr. Opin. Chem. Biol. 5 2001 567 571
21. R. Yazdanparast, F. Khodagholi, and R. Khodarahmi Artificial chaperone-assisted refolding of chemically denatured α-amylase Int. J. Biol. Macromol. 35 2005 257 263
22. H.A. Sathish, P.R. Kumar, and V. Prakash The differential stability of the left and right domains of papain Process Biochem. 44 2009 710 716
23. P) of pepsin Process Biochem. 44 2009 906 911
24. H. Ma, L. Huang, J. Jia, R. He, L. Luo, and W. Zhu Effect of energy-gathered ultrasound on alcalase Ultrason. Sonochem. 18 2011 419 424
25. M. Bashari, A. Eibaid, J. Wang, Y. Tian, X. Xu, and Z. Jin Influence of low ultrasound intensity on the degradation of dextran catalyzed by dextranase Ultrason. Sonochem. 20 2013 155 161
26. H. Hu, J. Wu, E.C.Y. Li-Chan, L. Zhu, F. Zhang, X. Xu, G. Fan, L. Wang, X. Huang, and S. Pan Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions Food Hydrocolloid. 30 2013 647 655
27. W.K. Surewicz, H.H. Mantsch, and D. Chapman Determination of protein secondary structure by fourier transform infrared spectroscopy: a critical assessment Biochemistry 32 1993 389 394
28. A. Barth Infrared spectroscopy of proteins Biochim. Biophys. Acta 1767 2007 1073 1101
29. 2O) solutions. I. Spectral parameters of amino acid residue absorption bands Biopolymers 30 1990 1243 1257
30. T.J. Mason, L. Paniwnyk, and J.P. Lorimer The uses of ultrasound in food technology Ultrason. Sonochem. 3 1996 S253 S260
31. H. Feng, G. Barbosa-Canovas, and J. Weiss Ultrasound technologies for food and bioprocessing R. Mawson, M. Gamage, N.S. Terefe, K. Knoerzer, Ultrasound in enzyme activation and inactivation 2010 Springer New York 369 404
32. I. Gülseren, D. Güzey, B.D. Bruce, and J. Weiss Structural and functional changes in ultrasonicated bovine serum albumin solutions Ultrason. Sonochem. 14 2007 173 183
33. K.K. Turoverov, and I.M. Kuznetsova Intrinsic fluorescence of actin J. Fluoresc. 13 2003 41 57
34. C.D. Geddes Reviews in fluorescence J.R. Albani, Origin of Tryptophan Fluorescence 2009 Springer New York 225 280
35. S.K. Chowdhury, J. Eshraghi, H. Wolfe, D. Forde, A.G. Hlavac, and D. Johnston Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: modifications of methionine and tyrosine Anal. Chem. 67 1995 390 398
36. T.W. Stone, N. Stoy, and L.G. Darlington An expanding range of targets for kynurenine metabolites of tryptophan Trends Pharmacol. Sci. 34 2013 136 143
37. P.K. Agarwal Enzymes: an integrated view of structure, dynamics and function Microb. Cell Fact. 5 2006 1 12
38. J. Song, W.Y. Tao, and W.Y. Chen Studies on the application of ultrasound in leather enzymatic unhairing Ultrason. Sonochem. 17 2010 376 382
39. Z.M. Tian, M.X. Wan, S.P. Wang, and J.Q. Kang Effects of ultrasound and additives on the function and structure of trypsin Ultrason. Sonochem. 11 2004 399 404
40. F. Franks Characterization of proteins F. Franks, Conformational stability: denaturation and renaturation 1988 Humana Press Inc. New Jersey 95 126
41. P. Sepulveda, J.R. Joseph Marciniszyn, D. Liu, and J. Tang Primary structure of porcine pepsin III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin J. Biol. Chem. 250 1975 5082 5088
42. D.F. Li, C.D. Mu, S.M. Cai, and W. Lin Ultrasonic irradiation in the enzymatic extraction of collagen Ultrason. Sonochem. 16 2009 605 609