Table of Contents Author Guidelines Submit a Manuscript
The Scientific World Journal
Volume 2014, Article ID 640949, 12 pages
http://dx.doi.org/10.1155/2014/640949
Research Article

Optimization of Processing Parameters for Extraction of Amylase Enzyme from Dragon (Hylocereus polyrhizus) Peel Using Response Surface Methodology

Department of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia (UPM), 43400 Serdang, Selangor, Malaysia

Received 1 March 2014; Revised 24 May 2014; Accepted 28 May 2014; Published 23 June 2014

Academic Editor: João B. T. Rocha

Copyright © 2014 Mehrnoush Amid et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. Lin, Y.-S. Lin, S.-T. Kuo, C.-M. Jiang, and M.-C. Wu, “Purification of soybean amylase by superparamagnetic particles,” Food Chemistry, vol. 117, no. 1, pp. 94–98, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. Y. Bai, H. Huang, K. Meng et al., “Identification of an acidic α-amylase from Alicyclobacillus sp. A4 and assessment of its application in the starch industry,” Food Chemistry, vol. 131, no. 4, pp. 1473–1478, 2012. View at Publisher · View at Google Scholar · View at Scopus
  3. A. Pandey, P. Nigam, C. R. Soccol, V. T. Soccol, D. Singh, and R. Mohan, “Advances in microbial amylases,” Biotechnology and Applied Biochemistry, vol. 31, no. 2, pp. 135–152, 2000. View at Google Scholar · View at Scopus
  4. S. Sivaramakrishnan, D. Gangadharan, K. M. Nampoothiri, C. R. Soccol, and A. Pandey, “α-amylases from microbial sources—an overview on recent developments,” Food Technology and Biotechnology, vol. 44, no. 2, pp. 173–184, 2006. View at Google Scholar · View at Scopus
  5. D. Stanley, K. J. F. Farnden, and E. A. MacRae, “Plant α-amylases: functions and roles in carbohydrate metabolism,” Biologia, vol. 60, no. 16, pp. 65–71, 2005. View at Google Scholar · View at Scopus
  6. Y. Dharmadi, Q. Chang, and C. E. Glatz, “Recovery of enzyme byproducts from potential plant hosts for recombinant protein production,” Enzyme and Microbial Technology, vol. 33, no. 5, pp. 596–605, 2003. View at Publisher · View at Google Scholar · View at Scopus
  7. F. C. Stintzing, A. Schieber, and R. Carle, “Betacyanins in fruits from red-purple pitaya, Hylocereus polyrhizus (Weber) Britton & Rose,” Food Chemistry, vol. 77, no. 1, pp. 101–106, 2002. View at Publisher · View at Google Scholar · View at Scopus
  8. L.-C. Wu, H.-W. Hsu, Y.-C. Chen, C.-C. Chiu, Y.-I. Lin, and J.-A. A. Ho, “Antioxidant and antiproliferative activities of red pitaya,” Food Chemistry, vol. 95, no. 2, pp. 319–327, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. R. Kammoun, B. Naili, and S. Bejar, “Application of a statistical design to the optimization of parameters and culture medium for α-amylase production by Aspergillus oryzae CBS 819.72 grown on gruel (wheat grinding by-product),” Bioresource Technology, vol. 99, no. 13, pp. 5602–5609, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Google Scholar · View at Scopus
  11. L. T. A. Ngo, T. L. Pham, and V. V. M. Le, “Purification of endopolygalacturonase from submerged culture of Aspergillus awamori L1 using a two-step procedure: enzyme precipitation and gel filtration,” International Food Research Journal, vol. 15, no. 2, pp. 135–140, 2008. View at Google Scholar · View at Scopus
  12. L. J. Derde, S. V. Gomand, C. M. Courtin, and J. A. Delcour, “Characterisation of three starch degrading enzymes: thermostable β-amylase, maltotetraogenic and maltogenic α-amylases,” Food Chemistry, vol. 135, no. 2, pp. 713–721, 2012. View at Publisher · View at Google Scholar · View at Scopus
  13. M. A. K. Azad, J.-H. Bae, J.-S. Kim et al., “Isolation and characterization of a novel thermostable α-amylase from Korean pine seeds,” New Biotechnology, vol. 26, no. 3-4, pp. 143–149, 2009. View at Publisher · View at Google Scholar · View at Scopus
  14. J. Li, Z. Jiang, H. Wu, L. Long, Y. Jiang, and L. Zhang, “Improving the recycling and storage stability of enzyme by encapsulation in mesoporous CaCO3-alginate composite gel,” Composites Science and Technology, vol. 69, no. 3-4, pp. 539–544, 2009. View at Publisher · View at Google Scholar · View at Scopus
  15. A. M. C. N. Rocha and A. M. M. B. Morais, “Characterization of polyphenoloxidase (PPO) extracted from “Jonagored” apple,” Food Control, vol. 12, no. 2, pp. 85–90, 2001. View at Publisher · View at Google Scholar · View at Scopus
  16. K. L. Chee, H. K. Ling, and M. K. Ayob, “Optimization of trypsin-assisted extraction, physico-chemical characterization, nutritional qualities and functionalities of palm kernel cake protein,” LWT—Food Science and Technology, vol. 46, no. 2, pp. 419–427, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. Y.-L. Chen, C.-K. Su, and B.-H. Chiang, “Optimization of reversed micellar extraction of chitosanases produced by Bacillus cereus,” Process Biochemistry, vol. 41, no. 4, pp. 752–758, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Agüloğlu Fincan, B. Enez, S. Özdemir, and F. Matpan Bekler, “Purification and characterization of thermostable α-amylase from thermophilic Anoxybacillus flavithermus,” Carbohydrate Polymers, vol. 102, pp. 144–150, 2014. View at Publisher · View at Google Scholar
  19. X. D. Liu and Y. Xu, “A novel raw starch digesting α-amylase from a newly isolated Bacillus sp. YX-1: purification and characterization,” Bioresource Technology, vol. 99, no. 10, pp. 4315–4320, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Shafiei, A.-A. Ziaee, and M. A. Amoozegar, “Purification and biochemical characterization of a novel SDS and surfactant stable, raw starch digesting, and halophilic α-amylase from a moderately halophilic bacterium, Nesterenkonia sp. strain F,” Process Biochemistry, vol. 45, no. 5, pp. 694–699, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Ueda, T. Asano, M. Nakazawa, K. Miyatake, and K. Inouye, “Purification and characterization of novel raw-starch-digesting and cold-adapted α-amylases from Eisenia foetida,” Comparative Biochemistry and Physiology, vol. 150, no. 1, pp. 125–130, 2008. View at Publisher · View at Google Scholar · View at Scopus
  22. R. Mukerjea, A. N. Gray, and J. F. Robyt, “Significant increases in potato starch-synthase and starch-branching-enzyme activities by dilution with buffer containing dithiothreitol and polyvinyl alcohol 50 K,” Carbohydrate Research, vol. 367, pp. 25–28, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. E. Riahi and H. S. Ramaswamy, “High pressure inactivation kinetics of amylase in apple juice,” Journal of Food Engineering, vol. 64, no. 2, pp. 151–160, 2004. View at Publisher · View at Google Scholar · View at Scopus
  24. G. S. Nerkar, Y. A. Chaudhari, and N. M. Khutle, “Extraction and characterization of alpha amylase from Phaseolus aconitifolius,” Current Pharma Research, vol. 1, no. 2, pp. 115–122, 2011. View at Google Scholar
  25. R. H. Sajedi, H. Naderi-Manesh, K. Khajeh et al., “A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104,” Enzyme and Microbial Technology, vol. 36, no. 5-6, pp. 666–671, 2005. View at Publisher · View at Google Scholar · View at Scopus
  26. A. S. M. Noman, M. A. Hoque, P. K. Sen, and M. R. Karim, “Purification and some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuber,” Food Chemistry, vol. 99, no. 3, pp. 444–449, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Tanaka and E. Hoshino, “Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillusα-amylases in a diluted anionic surfactant solution,” Journal of Bioscience and Bioengineering, vol. 93, no. 5, pp. 485–490, 2002. View at Publisher · View at Google Scholar · View at Scopus
  28. K. Chattopadhyay and S. Mazumdar, “Structural and conformational stability of horseradish peroxidase: effect of temperature and pH,” Biochemistry, vol. 39, no. 1, pp. 263–270, 2000. View at Publisher · View at Google Scholar · View at Scopus
  29. H. Lundqvist, G. S. Nilsson, A. C. Eliasson, and L. Gorton, “Changing the amylopectin-sodium dodecyl sulphate interaction by modifying the exterior chain length,” Stärke, vol. 54, pp. 100–107, 2002. View at Google Scholar
  30. S. Asada, S. F. Torabib, M. Fathi-Roudsaric, N. Ghaemia, and K. Khajehd, “Phosphate buffer effects on thermal stability and H2O2-resistance of horseradish peroxidase,” International Journal of Biological Macromolecules, vol. 48, no. 4, pp. 566–570, 2011. View at Publisher · View at Google Scholar