Foaming activity of lupin protein isolates in the absence of insoluble protein aggregates

[Display omitted] ▶ Albumin-rich protein isolate yields higher foamability than globulin-rich isolate. ▶ Regarding foam stability the two isolates show comparable performance. ▶ Foamability trends are alike with those measured in the presence of aggregates. ▶ Foam stability trends are different from...

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Veröffentlicht in:Colloids and surfaces. A, Physicochemical and engineering aspects Physicochemical and engineering aspects, 2011-06, Vol.382 (1), p.74-80
Hauptverfasser: Karapantsios, T.D., Papoti, V.T., Doxastakis, G.
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container_title Colloids and surfaces. A, Physicochemical and engineering aspects
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creator Karapantsios, T.D.
Papoti, V.T.
Doxastakis, G.
description [Display omitted] ▶ Albumin-rich protein isolate yields higher foamability than globulin-rich isolate. ▶ Regarding foam stability the two isolates show comparable performance. ▶ Foamability trends are alike with those measured in the presence of aggregates. ▶ Foam stability trends are different from those in the presence of aggregates. ▶ Electrical data give local information missed by global volumetric measurements. This study investigates the foaming properties of two lupin protein isolates (LPIs) extracted by ultrafiltration (albumin-rich fraction; LPTF) and isoelectric precipitation (globulin-rich fraction; LPTE), respectively. An earlier work on LPIs extracted by similar methods, Alamanou and Doxastakis [1], blamed the insoluble protein aggregates for the worse foamability and foam stability of the LPTE isolate compared to the LPTF isolate. Herein, the foaming properties of LPI are examined after removal of the insoluble fraction in order to appraise solely the effect of dissolved proteins. Foams are produced by whipping 1% w/v of LPIs aqueous solutions at pH 5.5 and 7, alone but also with addition of xanthan gum (0.05% and 0.1% w/v) and NaCl (0.1 M). Foaming ability and stability are assessed globally by volumetric measurements and locally by electrical conductance measurements taken non-intrusively at different heights along the foam. Both LPIs showed satisfactory foaming activity with electrical measurements depicting local drainage features that global volumetric measurements could not capture. It is found that LPTF yields better foamability than LPTE, exactly as it was shown earlier in the presence of aggregates. However, there is a discrepancy with that earlier work regarding foam stability since the two isolates perform comparably in the absence of aggregates. The discrepancy may be explained by considering that the larger size LPTE aggregates could have a stronger destabilizing effect than the smaller size LPTF aggregates. The role of pH, xanthan gum and NaCl in affecting the performance of the two LPIs is also discussed.
doi_str_mv 10.1016/j.colsurfa.2010.11.025
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This study investigates the foaming properties of two lupin protein isolates (LPIs) extracted by ultrafiltration (albumin-rich fraction; LPTF) and isoelectric precipitation (globulin-rich fraction; LPTE), respectively. An earlier work on LPIs extracted by similar methods, Alamanou and Doxastakis [1], blamed the insoluble protein aggregates for the worse foamability and foam stability of the LPTE isolate compared to the LPTF isolate. Herein, the foaming properties of LPI are examined after removal of the insoluble fraction in order to appraise solely the effect of dissolved proteins. Foams are produced by whipping 1% w/v of LPIs aqueous solutions at pH 5.5 and 7, alone but also with addition of xanthan gum (0.05% and 0.1% w/v) and NaCl (0.1 M). Foaming ability and stability are assessed globally by volumetric measurements and locally by electrical conductance measurements taken non-intrusively at different heights along the foam. Both LPIs showed satisfactory foaming activity with electrical measurements depicting local drainage features that global volumetric measurements could not capture. It is found that LPTF yields better foamability than LPTE, exactly as it was shown earlier in the presence of aggregates. However, there is a discrepancy with that earlier work regarding foam stability since the two isolates perform comparably in the absence of aggregates. The discrepancy may be explained by considering that the larger size LPTE aggregates could have a stronger destabilizing effect than the smaller size LPTF aggregates. 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A, Physicochemical and engineering aspects</title><description>[Display omitted] ▶ Albumin-rich protein isolate yields higher foamability than globulin-rich isolate. ▶ Regarding foam stability the two isolates show comparable performance. ▶ Foamability trends are alike with those measured in the presence of aggregates. ▶ Foam stability trends are different from those in the presence of aggregates. ▶ Electrical data give local information missed by global volumetric measurements. This study investigates the foaming properties of two lupin protein isolates (LPIs) extracted by ultrafiltration (albumin-rich fraction; LPTF) and isoelectric precipitation (globulin-rich fraction; LPTE), respectively. An earlier work on LPIs extracted by similar methods, Alamanou and Doxastakis [1], blamed the insoluble protein aggregates for the worse foamability and foam stability of the LPTE isolate compared to the LPTF isolate. Herein, the foaming properties of LPI are examined after removal of the insoluble fraction in order to appraise solely the effect of dissolved proteins. Foams are produced by whipping 1% w/v of LPIs aqueous solutions at pH 5.5 and 7, alone but also with addition of xanthan gum (0.05% and 0.1% w/v) and NaCl (0.1 M). Foaming ability and stability are assessed globally by volumetric measurements and locally by electrical conductance measurements taken non-intrusively at different heights along the foam. Both LPIs showed satisfactory foaming activity with electrical measurements depicting local drainage features that global volumetric measurements could not capture. It is found that LPTF yields better foamability than LPTE, exactly as it was shown earlier in the presence of aggregates. However, there is a discrepancy with that earlier work regarding foam stability since the two isolates perform comparably in the absence of aggregates. The discrepancy may be explained by considering that the larger size LPTE aggregates could have a stronger destabilizing effect than the smaller size LPTF aggregates. 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A, Physicochemical and engineering aspects</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karapantsios, T.D.</au><au>Papoti, V.T.</au><au>Doxastakis, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Foaming activity of lupin protein isolates in the absence of insoluble protein aggregates</atitle><jtitle>Colloids and surfaces. A, Physicochemical and engineering aspects</jtitle><date>2011-06-05</date><risdate>2011</risdate><volume>382</volume><issue>1</issue><spage>74</spage><epage>80</epage><pages>74-80</pages><issn>0927-7757</issn><eissn>1873-4359</eissn><abstract>[Display omitted] ▶ Albumin-rich protein isolate yields higher foamability than globulin-rich isolate. ▶ Regarding foam stability the two isolates show comparable performance. ▶ Foamability trends are alike with those measured in the presence of aggregates. ▶ Foam stability trends are different from those in the presence of aggregates. ▶ Electrical data give local information missed by global volumetric measurements. This study investigates the foaming properties of two lupin protein isolates (LPIs) extracted by ultrafiltration (albumin-rich fraction; LPTF) and isoelectric precipitation (globulin-rich fraction; LPTE), respectively. An earlier work on LPIs extracted by similar methods, Alamanou and Doxastakis [1], blamed the insoluble protein aggregates for the worse foamability and foam stability of the LPTE isolate compared to the LPTF isolate. Herein, the foaming properties of LPI are examined after removal of the insoluble fraction in order to appraise solely the effect of dissolved proteins. Foams are produced by whipping 1% w/v of LPIs aqueous solutions at pH 5.5 and 7, alone but also with addition of xanthan gum (0.05% and 0.1% w/v) and NaCl (0.1 M). Foaming ability and stability are assessed globally by volumetric measurements and locally by electrical conductance measurements taken non-intrusively at different heights along the foam. Both LPIs showed satisfactory foaming activity with electrical measurements depicting local drainage features that global volumetric measurements could not capture. It is found that LPTF yields better foamability than LPTE, exactly as it was shown earlier in the presence of aggregates. However, there is a discrepancy with that earlier work regarding foam stability since the two isolates perform comparably in the absence of aggregates. The discrepancy may be explained by considering that the larger size LPTE aggregates could have a stronger destabilizing effect than the smaller size LPTF aggregates. The role of pH, xanthan gum and NaCl in affecting the performance of the two LPIs is also discussed.</abstract><pub>Elsevier B.V</pub><doi>10.1016/j.colsurfa.2010.11.025</doi><tpages>7</tpages></addata></record>
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1873-4359
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source Elsevier ScienceDirect Journals
subjects Aggregates
aqueous solutions
chemical precipitation
colloids
drainage
Electrical conductivity
Foam ability
Foam stability
Foaming
foaming properties
Foams
Lupin
Lupins
Lupinus
Protein aggregates
protein isolates
Proteins
sodium chloride
Stability
ultrafiltration
whipping
Xanthan
xanthan gum
title Foaming activity of lupin protein isolates in the absence of insoluble protein aggregates
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