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A degradable biopolymer is an effective radiative cooling material.
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http://dx.doi.org/10.1126/science.adq5190 | DOI Listing |
Science
July 2024
State Key Laboratory of Structural Analysis, Optimization and CAE Software for Industrial Equipment, National Engineering Research Center for Advanced Polymer Processing Technology, Zhengzhou University, Zhengzhou 450002, People's Republic of China.
A degradable biopolymer is an effective radiative cooling material.
View Article and Find Full Text PDFAdv Colloid Interface Sci
December 2017
School of Physical Sciences, Jawaharlal Nehru University, New Delhi 110067, India; Special Center for Nanosciences, Jawaharlal Nehru University, New Delhi 110067, India. Electronic address:
In this review, a number of systems are described to demonstrate the effect of polyelectrolyte chain stiffness (persistence length) on the coacervation phenomena, after we briefly review the field. We consider two specific types of complexation/coacervation: in the first type, DNA is used as a fixed substrate binding to flexible polyions such as gelatin A, bovine serum albumin and chitosan (large persistence length polyelectrolyte binding to low persistence length biopolymer), and in the second case, different substrates such as gelatin A, bovine serum albumin, and chitosan were made to bind to a polyion gelatin B (low persistence length substrate binding to comparable persistence length polyion). Polyelectrolyte chain flexibility was found to have remarkable effect on the polyelectrolyte-protein complex coacervation.
View Article and Find Full Text PDFFood Chem
November 2016
New Hazardous Substance Team, Food Safety Evaluation Department, National Institute of Food and Drug Safety Evaluation, Ministry of Food and Drug Safety, 187 Osongsaengmyeong 2-ro, Osong-eup, Heungdeok-gu, Cheongju-si, Chungcheongbuk-do 28159, South Korea. Electronic address:
Gelatin, a purified protein derived mostly from pig skin and bovine tissue, is used widely in both food and pharmaceutical industries. Here, to determine the species of origin of capsule gelatin, we developed a sensitive and reliable test using the polymerase chain reaction (PCR) method, which included 1) species-specific or universal primer sets, designed to detect short 16S ribosomal RNA (rRNA) gene sequences from cow, pig, and fish (tilapia) as well as genes encoding the large subunit of plant ribulose-1,5-bisphosphate carboxylase oxygenase and 2) species-specific PCR coupled with whole-genome amplification. This method was used to verify manufacturing label claims of 28 gelatin capsule samples sold as dietary supplements.
View Article and Find Full Text PDFPhys Chem Chem Phys
August 2013
Polymer and Biophysics Laboratory, School of Physical Sciences, India.
The effect of persistence length on the intermolecular binding of DNA (200 bp, persistence length l(p) = 50 nm, polyanion) with three proteins, gelatin B (GB) (l(p) = 2 nm, polyampholyte chain), bovine serum albumin (BSA) (l(p) = 7 nm, polyampholyte colloid), gelatin A (GA) (l(p) = 10 nm, polyampholyte chain), and a polysaccharide chitosan (l(p) = 17 nm, polycation), was investigated in aqueous and in 1-methyl-3-octyl imidazolium chloride ionic liquid ([C8mim][Cl]) solutions. In DNA-GB and DNA-BSA solutions complexation primarily arises from surface patch binding whereas DNA-chitosan and DNA-GA binding was predominantly governed by electrostatic forces. These occurred at well defined pH values: (i) at pHc associative interactions ensued and soluble complexes were formed, (ii) at pHΦ soluble complexes coalesced to give rise to liquid-liquid phase separation (coacervation) and (iii) at pH(prep) formation of large insoluble complexes drove the solution towards liquid-solid phase separation.
View Article and Find Full Text PDFJ Phys Chem B
December 2012
Polymer and Biophysics Laboratory, School of Physical Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Study of kinetics of complex coacervation occurring in aqueous 1-octyl-3-methylimidazolium chloride ionic liquid solution of low charge density polypeptide (gelatin A) and 200 base pair DNA, and thermally activated coacervate into anisotropic gel transition, is reported here. Associative interaction between DNA and gelatin A (GA) having charge ratio (DNA:GA = 16:1) and persistence length ratio (5:1) was studied at fixed DNA (0.005% (w/v)) and varying GA concentration (C(GA) = 0-0.
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