SwePub - search: WFRF:(Belton P.S.)

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1.	Gillgren, Thomas, et al. (author) Plasticization of zein : A thermomechanical, FTIR, and dielectric study 2009 In: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 10:5, s. 1135-1139 Journal article (peer-reviewed)abstract Zein, the main seed storage protein of maize, has been widely studied as a possible source of material for the production of biodegradable plastic films. Plasticization of zein is critical to make functional films. While there have been a number of publications which report the behavior of systems with a wide variety of plasticizers, there have been few which attempt to examine the interactions of protein and plasticizer at the molecular level. In this paper, we report on the plasticizing effects of water, glycerol, and 2-mercaptoethanol, which were examined by a combination of spectroscopy (FTIR and dielectric) and thermomechanical methods. The results suggest that both water and glycerol are adsorbed onto the protein and form hydrogen bonds with the amide groups. The plasticizer then builds up in patches on the protein surface. 2-Mercaptoethanol only exhibited a weak plasticizing effect due probably to disulfide bond breaking. © 2009 American Chemical Society.

Gillgren, Thomas, et al. (author)
Plasticization of zein : A thermomechanical, FTIR, and dielectric study
2009
In: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 10:5, s. 1135-1139
Journal article (peer-reviewed)abstract
- Zein, the main seed storage protein of maize, has been widely studied as a possible source of material for the production of biodegradable plastic films. Plasticization of zein is critical to make functional films. While there have been a number of publications which report the behavior of systems with a wide variety of plasticizers, there have been few which attempt to examine the interactions of protein and plasticizer at the molecular level. In this paper, we report on the plasticizing effects of water, glycerol, and 2-mercaptoethanol, which were examined by a combination of spectroscopy (FTIR and dielectric) and thermomechanical methods. The results suggest that both water and glycerol are adsorbed onto the protein and form hydrogen bonds with the amide groups. The plasticizer then builds up in patches on the protein surface. 2-Mercaptoethanol only exhibited a weak plasticizing effect due probably to disulfide bond breaking. © 2009 American Chemical Society.

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