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Albumen Protein and Functional Properties of Gelation and Foaming

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Albumen Protein and Functional Properties of Gelation and Foaming Proteins of albumen functional properties 291 Review ALBUMEN PROTEIN AND FUNCTIONAL PROPERTIES OF GELATION AND FOAMING Ana Cláudia Carraro Alleoni R. Athaualpa Vaz de Melo, 179 - 13405-216 - Piracicaba, SP - Brasil. e-mail <[email protected]> ABSTRACT: Hen eggwhite proteins have been extensively utilized as ingredients in food processing because of their unique functional properties, such as gelling and foaming. This work reviews the molecular basis of the eggwhite proteins targeting the development of these functional properties during processing. Key words: ovalbumin, coagulation, gel, denaturation PROTEÍNAS DO ALBUME E PROPRIEDADES FUCIONAIS DE GELATINIZAÇÃO E FORMAÇÃO DE ESPUMA RESUMO: As proteínas da clara do ovo de galinha têm sido extensivamente usadas como ingredientes em alimentos processados, devido às suas propriedades funcionais, tais como gelatinização e formação de espuma. Essa revisão aborda as bases moleculares das proteínas da clara do ovo para o desenvolvimento dessas propriedades funcionais durante o processamento. Palavras-chave: ovalbumina, coagulação, gel, desnaturação INTRODUTION ALBUMEN PROTEINS The eggwhite has 9.7 to 12% protein (Vadehra Hen eggwhite have been extensively used as & Nath, 1973; Mine, 1995) and can be considered a sys- processed food ingredients, because of their functional tem built out of numerous globular proteins in an aque- properties of gelation and foam formation, ovalbumin ous solution. The seven largest fractions are ovalbumins proteins of chicken eggs have been used as processed A1 and A2, ovoglobulins G1, G2 and G3, ovomucoid and food ingredients (Mine, 1995). Gelation has evident conalbumin. Table 1 presents amounts of several pro- importance given the amount of available products to teins of eggwhite and some of their properties. consumers, such as desserts, puddings, reformulated 1. Ovalbumin meat products, tofu, and surimi. The success of many Ovalbumin constitutes 54% of eggwhite’s to- cooked food is related to protein coagulation, espe- tal protein (Zabik, 1992) and is its main protein cially the coagulation of egg proteins. Eggwhite and (Stevens, 1996). Vadehra & Nath (1973), Osuga & yolk can coagulate and act as linkage with other in- Feeney (1977), and Zabik (1992) report the existence gredients (Mine, 1995). of three ovalbumin fractions (A1, A2 and A3), detected Proteins make gels through ordinate polymer- by electrophoretic techniques. These fractions differ re- ization of molecules, providing a three-dimensional garding the phosphorus content of their molecules. network, and this process occurs by the transformation Ovalbumin A has two phosphate groups per molecule, of the viscous liquid in a viscous-elastic matrix 1 A2 has one group, and A3 has no phosphate group (Hermanssom, 1979). Foam is found in bread, cakes, (Vadehra & Nath, 1973; Zabik, 1992). Ovalbumin is a cookies, meringues, ice creams, and several bakery monomer, globular phospoglycoprotein with molecu- products. These products depend on air incorporation lar weight of 44.5 kDa, isoelectric point of 4.5, and to maintain their texture and structures during and af- has 385 residues from aminoacids (Nisbet et al., 1981), ter processing. The proteins encapsulate and retain air, half of them hydrophobic (Powrie & Nakai, 1985; improving the desirable textural attributes. The abil- Zabik, 1992; Mine, 1995). ity of protein to form and stabilize foam is related to Ovalbumin contains 3.5% carbohydrates and its amphiphilic behavior (polar/nonpolar) (Du et al., has four free sulphydrilic groups and a disulphide group. 2002). This study aims to review the molecular bases It can be denatured by heat exposure, by surface absorp- of ovalbumin proteins and their functional properties tion, in films, through agitation, or by the action of sev- of gel and foam formation and stabilization. eral denaturant agents (Vadehra & Nath, 1973). Sci. Agric. (Piracicaba, Braz.), v.63, n.3, p.291-298, May/June 2006 292 Alleoni Table 1 - Physical-chemical characteristics of albumen proteins (Source: Powrie & Nakai, 1985). Pnrotein APlbume ItMTolecular Weigh d Characteristic %adry weight DC° Ovalbumin 54.0 4.5 44,500 84.0 Fosfoglicoprotein Conalbumin 112.0 60. 707,70 6s1. Linkage with metal ion Ovomucoid 11.0 4.1 28,000 77.0 Inhibitory to trypsin Ovomucin 30.5 46.5-5. 5-n.5-8.3 x 10 Sialoprotei Lisozime 3.4 10.7 14,300 75.0 - Globulin G2 45.0 50. 459,00 9-2. Globulin G3 4.0 5.8 49,000 - - A5vidin 00.0 100. 6-8,30 Linkage with biotin e IP - isoelectric point; Td – denaturation temperature. During storage, ovalbumin is altered to s-oval- 2. Conalbumin or Ovotransferin bumin, an extra heat-stable form (denaturation at Conalbumin or ovotransferin is glycoprotein 92.5°C) in comparison to ovalbumin (denaturation at that represents 13% of eggwhite; its molecular weight 84.0°C), as determined by thermogram of the differ- varies from 60 to 95 kDa, with isoelectric point between ential scanning calorimeter (DSC) (Donovan & Mapes, 6.0 and 6.6 (Vadhera & Nath, 1973). Conalbumin can 1976). S-ovalbumin has a slightly lighter molecular bind to metal ions and form a protein-metal complex re- weight than ovalbumin and its relative quantity in the sistant to denaturation by heat, pressure, proteolitic en- eggwhite can increase during the storage period, from zymes, and denaturant agents (Azary & Feeney, 1958). 5% in fresh eggs to 81% after six months of refriger- This protein is complexed with two mols of metallic ion ated storage. Both pH and temperature also affect the per molecule with relative stability, and its ability to s-albumin formation (Vadehra & Nath, 1973). The s- bound to Fe is related to its antimicrobial activity. Con- ovalbumin dependency on pH indicates a step of ini- albumin has about 15 disulphide bindings and about tial ionization involving a sulphydrilic group and an 55% reactive residues (Zabik, 1992). amino group, or even the dependency on the concen- tration of hydroxyl ion, similar to an alkaline hydroly- 3. Ovomucoid sis (Smith & Back, 1965). The conversion of ovalbu- Ovomucoid is a glycoprotein bearing from 20 min to the extra stable form s-ovalbumin results from to 25% carbohydrates (Osuga & Feeney, 1977). It is differences in the structure of covalent bonding (Zabik, resistant to heat denaturation in acid solutions, and 1992). When eggs are covered with oil, coated with present inhibitory activity to trypsin (Stadelman & whey concentrate protein (Alleoni & Antunes, 2004), Coterril, 1973). Osuga & Feeney (1977) observed that or stored under refrigeration, this conversion is delayed ovomucoid from poultry eggs inhibits the bovine as a result of the lower carbon dioxide loss by the pores trypsin but not the human trypsin. Ovomucoid’s mo- of the egg shell. lecular weight varies from 26,100 to 28,300 Da, and Alleoni (1997) evaluated effects of storage its isoelectric point lies between 3.9 and 4.3 (Vadehra periods and two temperatures on poultry eggs. S-oval- & Nath, 1973). This protein is stabilized by hydropho- bumin contents registered were 18, 26 and 24% bic strengths and its high resistance to heat results from in eggs stored at 8°C for 7, 14 and 21 days, respec- its high cystine contents and, consequently, to the high tively. When stored at 25°C, eggs presented 56 and number of disulphide linkages – eight (Vadehra & 69% s-ovalbumin at 7 and 14 days, respectively. Nath, 1973). Smith & Back (1965) showed that 95% of ovalbumin is converted to s-ovalbumin when an ovalbumin so- 4. Ovomucin lution at pH 10 is kept and 55°C for 20 h. The maxi- Ovomucin is a glycosulphiprotein that contrib- mum production of s-ovalbumin occurs at pH 9.2 and utes to the gel-like structure of the eggwhite thick layer. the minimum at pH 7.9, both at 20°C (Nguyen & The eggwhite has two forms of ovomucin; the in- Smith, 1984). These refereed differences do not pro- soluble form characterizes the high viscosity of vide full explanation regarding the properties of s- eggwhite’s thin layer (Hayakawa & Sato, 1977). Ovo- ovalbumin, but properly exemplifies how little mucin presents from one to 2% of eggwhite’s total pro- changes in a given protein can significantly affect its teins (Vadehra & Nath, 1973), and differs from other properties. proteins because its molecule is extremely large and Sci. Agric. (Piracicaba, Braz.), v.63, n.3, p.291-298, May/June 2006 Proteins of albumen functional properties 293 contains sulphate esthers, large amounts of cystine (in- 1. Gelation terconnected through intermolecular linkages), and Gel is an intermediary form between solid and 50% of the total eggwhite sialic acid contents liquid. It is the cross-linking among polymeric mol- (Stadelman & Coterril, 1973). Ovomucin’s molecular ecules which make an intermolecular network within weight varies from 5.5 to 8.3 MDa. Ovomucin also has a liquid medium. In food systems, this liquid is water, a substantial amount of disulphide groups, and up to a solvent which affects the nature and the magnitude 33% carbohydrates (Vadehra & Nath, 1973). of intermolecular strengths that keep the integrity of the polymeric network. This network retains water, 5. Lysozyme avoiding losses (Oakenfull, 1987). Food processing Lysozyme is a glycoprotein, a single polypep- and the development of new products require ingredi- tide chain with 129 residues of aminoacids linked by ents such as the gelling agents, which build up a struc- four disulphide bonds, representing 3.5% of the tural matrix that supplies food’s desirable texture eggwhite; its molecular weight ranges from 14,300 to (Phillips et al., 1994). 14,600 Da, and its isoelectric point is 10.7 (Stadelman Gels can be described by their capacity to im- & Coterril, 1973). Lysozyme was previously placed in mobilize liquids, by their macromolecular structure, by the ovoglobulin group and referred to as G . Lysozyme’s 1 their texture, and by their rheological properties acid and basic lateral chains and terminal groups are dis- (Phillips et al., 1994).
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