Structural characterization of complexes prepared with glycerol monoestearate and maize starches with different amylose contents
Morphology and different structural features of V-amylose complexes prepared with different concentrations (1%, 2%, 3%) of glycerol monostearate (GMS) and normal maize (NMS), waxy maize (WMS), and high amylose maize (HAMS) starches were evaluated using X-ray diffraction, differential scanning calori...
| Authors: | , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2016 |
| Country: | Brasil |
| Institution: | Universidade Estadual Paulista (UNESP) |
| Repository: | Repositório Institucional da UNESP |
| Language: | English |
| OAI Identifier: | oai:repositorio.unesp.br:11449/168613 |
| Online Access: | http://dx.doi.org/10.1016/j.carbpol.2016.04.067 http://hdl.handle.net/11449/168613 |
| Access Level: | Open access |
| Keyword: | Amylopectin Emulsifier Inclusion complex Microscopy V-amylose |
| Summary: | Morphology and different structural features of V-amylose complexes prepared with different concentrations (1%, 2%, 3%) of glycerol monostearate (GMS) and normal maize (NMS), waxy maize (WMS), and high amylose maize (HAMS) starches were evaluated using X-ray diffraction, differential scanning calorimetry, scanning electronic microscopy (SEM), atomic force microscopy (AFM), and transmission electronic microscopy (TEM). There was inclusion complex formation between all starches and GMS regardless of emulsifier concentration, with exception of WMS-2%GMS and WMS-3%GMS samples. All of the inclusion complexes displayed a V-type crystalline pattern and endothermic dissociation peaks between 115 and 120 °C. They also displayed faceted crystalline structures with a tendency of the crystals to aggregate and form agglomerates of various sizes. TEM images of the complexes showed an aggregated strand structure interwoven with the GMS. Emulsifier and amylose quantities directly influenced complex formation. At high GMS concentrations, there was higher tendency of emulsifier to self-associate rather than form complexes with amylose. |
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