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Does macromolecular crowding compatible with enzyme stem bromelain structure and stability?
Int J Biol Macromol 2019; 131:527-535IJ

Abstract

It is essential to explore the impact of macromolecular crowding on protein in order to understand the behavior of the protein in the biological system. In this context, the consequences of macromolecular crowding on stem bromelain (BM) are explored, which is important for its industrial application. Herein, the effect of dextran (D70) and polyethylene glycol (P12 and P20) on native BM structure are investigated. The effect of crowder molecules on BM are deduced by combining the results of absorption, circular dichroism, fluorescence and activity studies. Additionally, molecular level interactions are investigated with molecular docking studies. Our results display that BM acts differently in higher and lower concentrations of crowding agents. Furthermore, crowding leads to alteration of protein structure and activity as compared to the dilute solutions. We observed that D70, is a very effective thermal stabilizing agent, while P12 is moderately stabilizing, on the other hand, P20 is destabilizing the BM structure. In the present study, the overall effect of crowders was destabilizing and deactivating on enzyme. Therefore, this study provides yet another example where soft interaction is dominating over the excluded volume effect.

Authors+Show Affiliations

Department of Chemistry, University of Delhi, Delhi 110 007, India.Department of Chemistry, University of Delhi, Delhi 110 007, India. Electronic address: pvenkatesu@chemistry.du.ac.in.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

30880059

Citation

Bhakuni, Kavya, and Pannuru Venkatesu. "Does Macromolecular Crowding Compatible With Enzyme Stem Bromelain Structure and Stability?" International Journal of Biological Macromolecules, vol. 131, 2019, pp. 527-535.
Bhakuni K, Venkatesu P. Does macromolecular crowding compatible with enzyme stem bromelain structure and stability? Int J Biol Macromol. 2019;131:527-535.
Bhakuni, K., & Venkatesu, P. (2019). Does macromolecular crowding compatible with enzyme stem bromelain structure and stability? International Journal of Biological Macromolecules, 131, pp. 527-535. doi:10.1016/j.ijbiomac.2019.03.090.
Bhakuni K, Venkatesu P. Does Macromolecular Crowding Compatible With Enzyme Stem Bromelain Structure and Stability. Int J Biol Macromol. 2019 Jun 15;131:527-535. PubMed PMID: 30880059.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Does macromolecular crowding compatible with enzyme stem bromelain structure and stability? AU - Bhakuni,Kavya, AU - Venkatesu,Pannuru, Y1 - 2019/03/15/ PY - 2019/02/04/received PY - 2019/03/06/revised PY - 2019/03/14/accepted PY - 2019/3/19/pubmed PY - 2019/9/10/medline PY - 2019/3/19/entrez KW - Enzyme assay KW - Macromolecular crowding KW - Protein stability KW - Spectroscopic analysis KW - Stem bromelain SP - 527 EP - 535 JF - International journal of biological macromolecules JO - Int. J. Biol. Macromol. VL - 131 N2 - It is essential to explore the impact of macromolecular crowding on protein in order to understand the behavior of the protein in the biological system. In this context, the consequences of macromolecular crowding on stem bromelain (BM) are explored, which is important for its industrial application. Herein, the effect of dextran (D70) and polyethylene glycol (P12 and P20) on native BM structure are investigated. The effect of crowder molecules on BM are deduced by combining the results of absorption, circular dichroism, fluorescence and activity studies. Additionally, molecular level interactions are investigated with molecular docking studies. Our results display that BM acts differently in higher and lower concentrations of crowding agents. Furthermore, crowding leads to alteration of protein structure and activity as compared to the dilute solutions. We observed that D70, is a very effective thermal stabilizing agent, while P12 is moderately stabilizing, on the other hand, P20 is destabilizing the BM structure. In the present study, the overall effect of crowders was destabilizing and deactivating on enzyme. Therefore, this study provides yet another example where soft interaction is dominating over the excluded volume effect. SN - 1879-0003 UR - https://www.unboundmedicine.com/medline/citation/30880059/Does_macromolecular_crowding_compatible_with_enzyme_stem_bromelain_structure_and_stability L2 - https://linkinghub.elsevier.com/retrieve/pii/S0141-8130(19)30909-2 DB - PRIME DP - Unbound Medicine ER -