Inactivation of Lysozyme by Native Ovalbumin

Cunningham, F. E.; Lineweaver, Hans

doi:10.3382/ps.0461471

Cited by 35 publications

(10 citation statements)

References 23 publications

(20 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since acylation reactions have the net effect of increasing charge uniformity, it is suggested that the apparent increase in activity of lysozyme may be the result of a greater level of free lysozyme available for reaction. The availability of lysozyme may be due to replusion of like charges, resulting in dissociation of electrostatic lysozymeprotein interactions described by Cunningham and Lineweaver (1967) and Cotterill and Winter (1955). Decreases in optical densities of egg white (Table 1) as the level of acylation increased indicates aggregation or protein-protein interactions were reduced (Hcrmansson, 1979).…”

Section: Resultsmentioning

confidence: 97%

Acylation of Egg White Proteins with Acetic Anhydride and Succinic Anhydride

Ball

1982

Poultry Science

View full text Add to dashboard Cite

Egg white was acylated with acetic anhydride and succinic anhydride. Addition of 5, 10, 15, 20, and 25 moles of acylating reagent per 50,000 g of egg white protein modified 10, 24, 40, 48, and 60% of the free amino groups, respectively. Functional group analyses indicated that the phenolic group of tyrosine and the hydroxyl groups of serine and threonine did not react with the anhydrides. Sulfhydryl groups were modified 1 to 6% at the 25 mole level of acetic and succinic anhydride, respectively. Conalbumin's ability to complex iron was impaired. Lysozyme was inactivated at levels of addition above 10 m of succinic anhydride and at levels of added acetic anhydride above 20 m. Polyacrylamide electrophoretograms indicated that considerable protein charge alteration occurred. Succinylated egg white exhibited improved heat stability and foaming ability, and there was no change in angel cake performance. Acetylation diminished heat stability, improved foaming ability, and at the 20 mole level diminished performance in angel cakes. These results show that chemical and functional properties of egg white protein can be significantly altered by relatively mild acylation reactions. (

show abstract

Section: Resultsmentioning

confidence: 97%

Acylation of Egg White Proteins with Acetic Anhydride and Succinic Anhydride

Ball

1982

Poultry Science

View full text Add to dashboard Cite

show abstract

“…Lysozyme-ovalbumin interaction has been proved to cause the loss of lysozyme enzymatic activity in thermal conditions. [6] It was also suggested that the inhibition of lysozyme muramidase activity may happen due to the formation of rigid aggregates of ovalbumin and lysozyme rather than the configuration changes of lysozyme itself. [18] It is interesting to find that, in our previous study, the abundance of one spot (experimental MW is 66.1 kDa) representing ovalbumin-lysozyme complex continued to increase during the early incubation period at 38°C in fertilised eggs while remained stable after two days of storage in unfertilised eggs.…”

Section: Discussionmentioning

confidence: 99%

“…[5] In an early study, ovalbumin was found to remarkably influence the rate of inactivation of lysozyme at temperatures which caused no observable denaturation when the two proteins were heated separately. [6] The sulfhydryl groups of ovalbumin were implicated in the inactivation of lysozyme, probably via the reduction of one or more disulfide bonds. [6] The heat-induced interaction of the egg white lysozyme with N-ovalbumin was also proved to form amyloid-like fibrils.…”

Section: Introductionmentioning

confidence: 99%

“…[6] The sulfhydryl groups of ovalbumin were implicated in the inactivation of lysozyme, probably via the reduction of one or more disulfide bonds. [6] The heat-induced interaction of the egg white lysozyme with N-ovalbumin was also proved to form amyloid-like fibrils. [7] Also, the heat-induced interaction between ovalbumin and ovotransferrin at 65°C was investigated through turbidity development and polyacrylamide gel electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of candidate proteins interacted with ovalbumin during the early phase of embryonic development

Pan

Qiu

Zhao

et al. 2017

International Journal of Food Properties

View full text Add to dashboard Cite

In the present study, protein complexes emerged in high molecular weight (MW) region (95-170 kDa) were observed in fertilised chicken egg white after 7 days of incubation. Investigations were performed to reveal the possible proteins involved in these complexes. The emerged 10 protein bands from SDS-PAGE gel were confirmed to be ovalbumin through matrix-assisted laser desorption/ionisation time-of-flight tandem mass spectrometry (MALDI-TOF MS/MS) followed by Western blot analysis. To reveal the possible interactions among ovalbumin and other egg white proteins, LC connected to LTQ-Orbitrap mass spectrometer was used. Besides ovalbumin, 11 egg white proteins were identified including ovotransferrin, lysozyme, ovalbumin-related protein X, ovalbumin-related protein Y, hep21, alpha-enolase, ovoinhibitor, and a protein similar to ryanodine receptor 1. These results indicated widespread thermal-induced protein interactions among ovalbumin and other egg white proteins.

show abstract

“…It is suggested from this result that the reactivity of sulfhydryl groups in ovalbumin was enhanced by the addition of lysozyme. Cunningham and Lineweaver 11 ) have reported that in the case of inactivation of lysozyme by ovalbumin during heating, the sultbydryl groups of ovalbumin were implicated in the reduction of the disulfide bond in lysozyme. The participation of sulfhydryl groups of ovalbumin in the heatinduced aggregation was further confirmed from results of the dissociation into ovalbumin and lysozyme of the aggregates in the presence of 2-mercaptoethanol ( Fig.…”

Section: Changes Of Sulfhydryl Groups In Proteins During Heatingmentioning

confidence: 99%