Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Dynamic measurements of ?-lactoglobulin structures during aggregation, gel formation and gel break-up in mixed biopolymer systems
SIK – Institutet för livsmedel och bioteknik.
SIK – Institutet för livsmedel och bioteknik.
2002 (English)In: Food Hydrocolloids, ISSN 0268-005X, E-ISSN 1873-7137, Vol. 16, no 5, 477-488 p.Article in journal (Refereed)
Abstract [en]

The kinetics of aggregation and gelation of ?-lactoglobulin/amylopectin microstructures have been studied by using confocal laser scanning microscopy (CLSM) equipped with a temperature stage, transmission electron microscopy (TEM) and dynamic mechanical analysis in shear. The behaviour of the final gels was studied during fracture deformations using a tensile stage adapted to the CLSM. The different types of particulate ?-lactoglobulin (?-1g) network structures were generated by adding non-gelling amylopectin of varying concentration and viscosity. The results showed that the higher the concentration and the higher the viscosity of the amylopectin, the lower the temperature required for ?-1g to aggregate into particle aggregates and clusters visible in the CLSM. The gelling temperature of the ?-1g, determined by small deformation rheological measurements, was also found to decrease with increase in amylopectin concentration. However, although an increased concentration of amylopectin accelerated the particle aggregation of ?-1g, amylopectin with a higher viscosity was found to restrict the aggregated protein aggregates and clusters to form a connected protein network. The result of the difference in connectivity was shown when the gel structures were studied during fracture deformations in tension. In the weaker gel type, where the continued aggregation to a connected network had been obstructed, the fracture was extended more deeply inside the structure than in the stronger gel type with good connectivity, when exposed to the same deformation. The distribution of the protein and the amylopectin in the aggregated structure was visualized by TEM. Amylopectin was found inside the ?-1g aggregates in the gels containing a lower viscosity of the amylopectin. In gels containing amylopectin with higher viscosity, the amylopectin was found in the pores between the protein networks, separated from the protein phase. © 2002 Elsevier Science Ltd. All rights reserved.

Place, publisher, year, edition, pages
2002. Vol. 16, no 5, 477-488 p.
Keyword [en]
Food Engineering
Keyword [sv]
Livsmedelsteknik
National Category
Food Science
Identifiers
URN: urn:nbn:se:ri:diva-8600DOI: 10.1016/S0268-005X(01)00125-4OAI: oai:DiVA.org:ri-8600DiVA: diva2:966473
Available from: 2016-09-08 Created: 2016-09-08Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full texthttp://www.scopus.com/inward/record.url?eid=2-s2.0-0036324491&partnerID=40&md5=87cc5033cca0cb99163005f1239585ad
By organisation
SIK – Institutet för livsmedel och bioteknik
In the same journal
Food Hydrocolloids
Food Science

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 9 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
v. 2.27.0