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Systematic kinetics of melt-blended Polylactic acid (PLA)/Polybutylene succinate (PBS) and PLA/PBS/functionalized chitosan (FCH) nanobiocomposites with dicumyl peroxide (DCP) and chemical changes thereof at degradation temperatures are evaluated using thermogravimetry (TGA) and thermogravimetry coupled to Fourier transform infrared spectroscopy (TGA-FTIR). A comprehensive kinetic model is employed on above blended samples, including (i) Flynn-Wall-Ozawa, Kissinger, Kissinger-Akahira-Sunose methods to investigate the kinetic and thermodynamic variables, and (ii) Generalized master plots to propose the thermal-induced mechanism. The thermal stability of PLA/PBS reduced with increasing FCH loading up to 3 wt%, and improved for DCP treated PLA/PBS/1FCH at maximum degradation temperature (T) is noticed. The activation energy estimated from Flynn-Wall-Ozawa method are (129-139 kJmol), (116-152 kJmol), (109-146 kJmol), (132-169 kJmol) and (120-166 kJmol) for PLA/PBS, PLA/PBS/1FCH, PLA/PBS/3FCH, PLA/PBS/1DFCH and PLA/PBS/3DFCH respectively. The generalized master plots depicts that the PLA/PBS blend exhibited L2-F1 mechanism whereas their nanobiocomposite with or without DCP followed L2-D and A2-L2-D mechanism respectively. Coupled TGA-FTIR highlights the similar kinds of products such as lactide, acetaldehyde, esters, CO and CO liberated during the thermal degradation of PLA/PBS blend and their nanobiocomposites. These crosslinked/branched structures are postulated by the rheological behavior which confirmed increase in the complex viscosity (η*) and storage modulus (G') of PLA/PBS/D/1FCH.
This article was published in the following journal.
Name: International journal of biological macromolecules
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A poly(A) binding protein that is involved in promoting the extension of the poly A tails of MRNA. The protein requires a minimum of ten ADENOSINE nucleotides in order for binding to mRNA. Once bound it works in conjunction with CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR to stimulate the rate of poly A synthesis by POLY A POLYMERASE. Once poly-A tails reach around 250 nucleotides in length poly(A) binding protein II no longer stimulates POLYADENYLATION. Mutations within a GCG repeat region in the gene for poly(A) binding protein II have been shown to cause the disease MUSCULAR DYSTROPHY, OCULOPHARYNGEAL.
A poly(ADP-ribose) polymerase that contains two ZINC FINGERS in its N-terminal DNA-binding region. It modifies NUCLEAR PROTEINS involved in chromatin architecture and BASE EXCISION REPAIR with POLY ADENOSINE DIPHOSPHATE RIBOSE.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.
Post-translational modification of proteins with POLY ADENOSINE DIPHOSPHATE RIBOSE.