International journal of


EISSN: 2313-3724, Print ISSN:2313-626X

Frequency: 12

line decor
line decor

 Volume 4, Issue 12 (December 2017), Pages: 31-35


 Original Research Paper

 Title: Tertiary structure prediction of bromelain from Ananas Comosus using comparative modelling method

 Author(s):  Fatahiya Mohamed Tap 1, Fadzilah Adibah Abd Majid 2, *, Nurul Bahiyah Ahmad Khairudin 1


 1Chemical Energy Conversion and Applications Group, Malaysia Japan International Institute of Technology, Universiti Teknologi Malaysia, Kuala Lumpur, Malaysia
 2Institute of Marine Biotechnology, Universiti Malaysia Terengganu, 21030 Kuala Terengganu, Malaysia

 Full Text - PDF          XML


Bromelain is a general name for a family of sulfhydryl which can be found in the proteolytic enzyme group from pineapples (Ananas Comosus).  This study focuses on the prediction of three dimensional structures (3D) of stem bromelain using the method of comparative modelling. The amino acid sequence of bromelain was obtained from the NCBI database was used as a tool to search for proteins with known 3D structures related to the target sequence. Suitable template was chosen based on >30% sequence similarity and lowest e-value. Based on these criteria, 1YAL was selected as the best template with 55% of sequence similarity and 9x10-52 of e-value. 

 © 2017 The Authors. Published by IASE.

 This is an open access article under the CC BY-NC-ND license (

 Keywords: Bromelain, Comparative modelling, Sequence alignment

 Article History: Received 21 February 2017, Received in revised form 2 October 2017, Accepted 8 October 2017

 Digital Object Identifier:


 Tap FM, Majid FAA, Khairudin NBA (2017). Tertiary structure prediction of bromelain from Ananas Comosus using comparative modelling method. International Journal of Advanced and Applied Sciences, 4(12): 31-35

 Permanent Link:


 References (17)

  1. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, and Lipman DJ (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Research, 25(17): 3389-3402. PMid:9254694 PMCid:PMC146917 
  2. Apweiler R, Bairoch A, and Wu CH (2004). Protein sequence databases. Current Opinion in Chemical Biology, 8(1): 76-80.  PMid:15036160 
  3. Arshad ZIM, Amid A, Yusof F, Jaswir I, Ahmad K, and Loke SP (2014). Bromelain: An overview of industrial application and purification strategies. Applied Microbiology and Biotechnology, 98(17): 7283-7297.  PMid:24965557 
  4. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, and Bourne PE (2000). The protein data bank. Nucleic Acids Research, 28(1): 235-242.  PMid:10592235  PMCid:PMC102472 
  5. Colovos C and TO Yeates (1993). Verification of protein structures: Patterns of nonbonded atomic interactions. Protein Science, 2(9): 1511-1519. PMid:8401235  PMCid:PMC2142462     
  6. Gautam SS, Mishra SK, Dash V, Goyal AK, and Rath G (2010). Comparative study of extraction, purification and estimation of bromelain from stem and fruit of pineapple plant. Thai Journal of Pharmaceutical Sciences, 34(2): 67-76.     
  7. Huang X and Miller W (1991). A time-efficient, linear-space local similarity algorithm. Advances in Applied Mathematics, 12(3): 337-357.
  8. Humphrey W, Dalk A, and Schulten K (1996) VMD: Visual molecular dynamics. Journal of Molecular Graphics, 14(1): 33-38. 
  9. Luthy R, Bowie JU, and Eisenberg D (1992). Assessment of protein models with three-dimensional profiles. Nature, 356(6364): 83-85.  PMid:1538787 
  10. Maes D, Bouckaert J, Poortmans F, Wyns L, and Looze Y (1996). Structure of chymopapain at 1.7 A resolution. Biochemistry, 35(50): 16292-16298.  PMid:8973203     
  11. Morris AL, MacArthur MW, Hutchinson EG, and Thornton JM (1992). Stereochemical quality of protein structure coordinates. Proteins: Structure, Function and Bioinformatics, 12(4): 345-364. PMid:1579569 
  12. Pavan R, Jain S, Shraddha, and Kumar A (2012). Properties and therapeutic application of bromelain: A review. Biotechnology Research International, 2012: Article ID 976203, 6 pages.  PMid:23304525  PMCid:PMC3529416 
  13. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, and Ferrin TE (2004). UCSF Chimera--a visualization system for exploratory research and analysis. Journal of Computational Chemistry, 25(13): 1605-1612.  PMid:15264254 
  14. Pruitt K, Brown G, Tatusova T, and Maglott D (2002). The reference sequence (RefSeq) database. In: McEntyre J and Ostell J (Eds.), The NCBI handbook, National Center for Biotechnology Information: 1-24. Bethesda Softworks, Rockville, USA.     
  15. Roy A and Zhang Y (2012). Recognizing protein-ligand binding sites by global structural alignment and local geometry refinement. Strcucture, 20(6): 987-997.  PMid:22560732  PMCid:PMC3372652     
  16. Šali A and Blundell TL (1993). Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology, 234(3): 779-815. PMid:8254673     
  17. Shen MY and Sali A (2006). Statistical potential for assessment and prediction of protein structures. Protein Science, 15(11): 2507–2524. PMid:17075131 PMCid:PMC2242414