The Gelation Of Proteins

Ziegler, Gregory R.; Foegeding, E. Allen

doi:10.1016/s1043-4526(08)60008-x

Cited by 351 publications

(251 citation statements)

References 192 publications

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“…8b by the presence of two different trends. This last spectral component is attributed to the formation of very strong intermolecular H-bonds [44,60,69] and we suggest that the specific presence of copper may promote, in a very short time, the formation of heat-induced network ready to form macromolecules and/or gels, as reported for many globular protein, such as BLG [70,71]. As it is shown in Fig.…”

Section: Accepted M Manuscriptsupporting

confidence: 76%

Thermal aggregation of β-lactoglobulin in presence of metal ions

Navarra

Leone

Militello

2007

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT AbstractIn this work, we report a study on the effects of zinc and copper ions on the heat-induced aggregation of β−Lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FT-IR absorption measurementsshow the different role played by two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than the copper. Then, fixed the temperature, formation of a large amount of aggregates, with a large dimension, is observed for the Zn-BLG in shorter time; on the contrary, the presence of the copper in solution does not affect the aggregation process but the secondary structure changes and the formation of different stronger intermolecular H-bonds, which probably lead to build a network of bonds that takes towards gelation. Our studies show as time evolution of aggregation process of BLG is dramatically affected by the presence of metal ions in solution and structural protein modifications are induced by different divalent metal ions.

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Section: Accepted M Manuscriptsupporting

confidence: 76%

Thermal aggregation of β-lactoglobulin in presence of metal ions

Navarra

Leone

Militello

2007

Biophysical Chemistry

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“…Up until the latter half of the 1990s, sarcoplasmic protein (SP), a water-soluble muscle protein, was believed to contribute very little to the texture of meat products (Samejima et al, 1969;Asghar et al, 1985;Ziegler and Foegeding, 1990). However, recently, a number of reports have shown improved texture of meat products by the addition of SP.…”

Section: Introductionmentioning

confidence: 99%

Molecular Interaction Studies Evaluating the Gelation of Myosin B with Glyceraldehyde 3-phosphate Dehydrogenase after Succinylation

Sakamoto

Sasaki

Nakade

et al. 2013

FSTR

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Previously, it was clarified that myofibril gelation was enhanced by the basic protein glyceraldehyde 3-phosphate dehydrogenase (GPD). In this study, the mechanism of the gel-enhancing action of GPD to myosin B was evaluated through the study of the surface properties of GPD. GPD and myosin B were prepared from pork loin. Succinylated GPD (S-GPD) was successfully prepared without any loss of solubility at a weight ratio (succinic anhydrate to GPD) of 1.0. Though gelation of myosin B alone required a minimum protein concentration of 4.0% (w/v), the addition of GPD enhanced the gelation of myosin B at a concentration of 3.5% (w/v). Furthermore, GPD increased the gel strength drastically at concentrations above 4.5% (w/v). On the other hand, the addition of S-GPD did not improve the gelling property of myosin B. SDS-PAGE showed molecular interaction between GPD and myosin B, but not between S-GPD and myosin B. However, in the case of GPD, the GPD band became insoluble under coexistence of GPD with myosin B. Meanwhile, the myosin heavy chain was partially soluble. Furthermore, actin and GPD bands became thicker in the insoluble fraction after mixing of G-actin and GPD. These results indicate that positive charges on the surface of GPD are necessary to enhance the gelation of myosin B.

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“…In particular, this may result from changes in the protonation of the three histidine residues (His12, His38, and His42) upon raising the pD above 6. The heat-induced denaturation of bound pediocin leads to an irreversible self-aggregation that is more extensive as the pD increases from 7 to 8 due to the decrease in the intermolecular electrostatic repulsions (77). In the presence of DMPG at pD 6, the thermal behavior of pediocin is different from that observed for the peptide alone.…”

Section: Discussionmentioning

confidence: 92%

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Gaussier

Lefèvre

Subirade

2003

Appl Environ Microbiol

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To obtain molecular insights into the action mode of antimicrobial activity of pediocin PA-1, the interactions between this bacteriocin and dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylglycerol (DMPG) model membranes have been investigated in D 2 O at pD 6 by Fourier transform infrared spectroscopy. The interactions were monitored with respect to alteration of the secondary structure of pediocin, as registered by the amide I band, and phospholipid conformation, as revealed by the methylene s (CH 2 ) and carbonyl (CAO) stretching vibrations. The results show that no interaction between pediocin and DMPC occurs. By contrast, pediocin undergoes a structural reorganization in the presence of DMPG. Upon heating, pediocin self-aggregates, which is not observed for this pD in aqueous solution. The gel-to-crystalline phase transition of DMPG shifts to higher temperatures with a concomitant dehydration of the interfacial region. Our results indicate that pediocin is an extrinsic peptide and that its action mechanism may lie in a destabilization of the cell membrane.Pediocin PA-1 is a 44-amino-acid (molecular mass, 4,629 Da; pI, 9.6) (35) class IIa bacteriocin (38) produced by Pediococcus acidilactici PAC 1.0 and naturally found in fermented sausages (37) or other meat and vegetable fermentations (5). Its sequence is highly homologous to other class IIa bacteriocins (59). The N-terminal 20-amino-acid half of pediocin is in the majority of cases polar or cationic and highly conserved, with the consensus sequence Y3-G4-N5-G6-V7. The C-terminal half (residues A21 to C44) is much less polar and less conserved, containing a hypothetical hydrophobic membrane interaction domain. Two disulfide bonds stabilize the peptide structure, the one between the residues 24 and 44 accounting for its broad range of antimicrobial activity (17). Because of its specific antimicrobial activity against the foodborne psychrotrophic pathogen Listeria monocytogenes, pediocin PA-1 can potentially serve as a nontoxic food preservative to improve the quality, naturalness, and safety (55) of dairy and meat products.The data for Listeria innocua death induced by pediocin PA-1 reveal that its activity maximum is reached near pD 6 and decreases at pD 7 and 8 (15, 30). A relation between activity and structure alterations has not yet been completely established. The loss of activity as a function of pD seems to be associated to a structural reorganization and a decrease in the protein flexibility that in turn results in an irreversible aggregation upon heating (30). The C-terminal region is first involved in the aggregation process, resulting in a total inactivation of the protein (30). The N-terminal region participates in the aggregation process in a second step. Pediocin can exist in a soluble and hydrophobic structural form (16). In an aqueous environment, pediocin presents an unordered structure as seen by circular dichroism (75) and Fourier transform infrared (FTIR) spectroscopy (30), whereas upon adsorption to vesicles, a structura...

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The Gelation Of Proteins

Cited by 351 publications

References 192 publications

Thermal aggregation of β-lactoglobulin in presence of metal ions

Thermal aggregation of β-lactoglobulin in presence of metal ions

Molecular Interaction Studies Evaluating the Gelation of Myosin B with Glyceraldehyde 3-phosphate Dehydrogenase after Succinylation

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

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