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How does bovine serum albumin sustain in saccharomate® derived from pine tree biomass?

  • Yadav, Niketa1
  • Umapathi, Reddicherla1
  • Venkatesu, Pannuru2
  • 1 Department of Chemistry, University of Delhi, Delhi, 110 007, India. , (India)
  • 2 Department of Chemistry, University of Delhi, Delhi, 110 007, India. Electronic address: [email protected] , (India)
Published Article
Colloids and surfaces. B, Biointerfaces
Publication Date
Mar 23, 2020
DOI: 10.1016/j.colsurfb.2020.110975
PMID: 32213431


Nowadays, research on renewable raw materials and bioresources is a new concern towards the promotion of sustainable process and product development. The use of various plant biomasses such as starch, lignocellulosic and saccharide can be considered as an alternative for using cheaper and less polluting raw materials. In this regard, pine tree biomass, a lignocellulosic forest residue that has various value-added importance and it acts as a model of economic value to the agro-industrial fields. On the other hand, in order to meet and address the challenges of ever-increasing demands of bioresources, there has been significant research interest in deciphering the molecular interactions between proteins and biomass derived substances. No study reports the significance of saccharomate® derived from pine tree biomass on the structural and thermal stability of proteins. There is a sizable interest in the interactions between proteins and biomass derived substances, owing to their utilization and applications. Herein, we used various biophysical techniques such as absorption spectroscopy, fluorescence spectroscopy, circular dichroism (CD) and dynamic light scattering (DLS) to study the impact of pine tree biomass derived saccharomate® (PBDS) on bovine serum albumin (BSA). Further for better understanding of morphological changes of BSA in presence of biomass, Transmission electron microscopy (TEM) was also studied. The present study revealed that the increasing concentration of saccharomate® perturbs structural stability however; the thermal stability of BSA remained unchanged. The transition temperature of BSA remained approximately same in presence of different concentrations of PBDS. Furthermore, the size of BSA increases from 9.22 nm to 135.58 nm in presence of higher concentration of PBDS as revealed by DLS studies. To the best of our knowledge, the results represent first detailed proof of the unusual effect of PBDS on the model protein BSA. Copyright © 2020 Elsevier B.V. All rights reserved.

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