Relationship of Composition to Protein Functionality

Fligner, Karen; Mangino, M.E.

doi:10.1021/bk-1991-0454.ch001

Cited by 26 publications

(25 citation statements)

References 19 publications

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“…However, the emulsification capacity of the collagen hydrolysates generally increased significantly at pH 7.0 as compared with those at pH 4.0 (P< 0.05). This may be due to increased exposition of hydrophilic and hydrophobic residues of the hydrolysates at higher pH values, which promotes a major interaction at the oil-in-water (O:W) interface (Flinger and Mangino, 1991). The fraction with a molecular weight of < 3 kDa generally showed lower EAI and ESI at pH 7.0 and pH 10.0 than those of the 3−10 kDa, and >10 kDa fraction (P< 0.05).…”

Section: Functional Properties Of Hydrolysatesmentioning

confidence: 99%

Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates

Liu

Su²,

Zeng³

2011

J. Ocean Univ. China

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Giant red sea cucumber (Parastichopus californicus) is an under-utilized species due to its high tendency to autolysis. The aim of this study was to evaluate the functional properties of collagen hydrolysates from this species. The degree of hydrolysis (DH), amino acid composition, SDS-PAGE, emulsion activity index (EAI), emulsion stability index (ESI), foam expansion (FE), and foam stability (FS) of hydrolysates were investigated. The effects of pH on the EAI, ESI FE and FS of hydrolysates were also investigated. The results indicated that the β and α 1 chains of the collagen were effectively hydrolyzed by trypsin at 50℃ with an Enzyme/Substrate (E/S) ration of 1:20 (w:w). The DH of collagen was up to 17.3% after 3 h hydrolysis with trypsin. The hydrolysates had a molecular weight distribution of 1.1−17 kDa, and were abundant in glycine (Gly), proline (Pro), glutamic acid (Glu), alanine (Ala) and hydroxyproline (Hyp) residues. The hydrolysates were fractionated into three fractions (< 3 kDa, 3−10 kDa, and > 10 kDa), and the fraction of 3−10 kDa exhibited a higher EAI value than the fraction of > 10 kDa (P<0.05). The fraction of > 10 kDa had higher FE and FS values than other fractions (P<0.05). The pH had an important effect on the EAI, ESI, FE and FS. All the fractions showed undesirable emulsion and forming properties at pH 4.0. Under pH 7.0 and pH 10.0, the 3−10 kDa fraction showed higher EAI value and the fraction of > 10 kDa showed higher FE value, respectively. They are hoped to be utilized as functional ingredients in food and nutraceutical industries.

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Section: Functional Properties Of Hydrolysatesmentioning

confidence: 99%

Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates

Liu

Su²,

Zeng³

2011

J. Ocean Univ. China

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“…The EAI is a function of oil volume fraction, protein concentration and type of equipment used to produce the emulsion (Flinger and Mangino 1991). The mechanism of the emulsification process is the absorption of proteins to the surface of freshly formed oil droplets during homogenisation, forming a protective membrane preventing droplets from coalescing.…”

Section: Emulsifying Propertiesmentioning

confidence: 99%

Valorisation of smooth hound (Mustelus mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides

Sayari

Sila

Haddar

et al. 2015

Environ Sci Pollut Res

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Concerns over the environmental and waste disposal problems created by the large amounts of by-products generated from fish processing industries are increasing worldwide. The bioconversion of those marine waste by-products through the enzymatic hydrolysis of their protein content offers the possibility for the development of bioactive peptides for use in various biotechnological applications. The present study aimed to investigate and evaluate the biological and functional properties of smooth hound (Mustelus mustelus) protein hydrolysates (SHPHs) obtained by treatment with intestinal and gastric enzyme preparations from M. mustelus viscera and porcine pancreatin. The results revealed that the SHPHs exhibited different degrees of hydrolysis and antioxidant activity. The hydrolysate produced by the intestinal crude extract presented the highest rate of antioxidative activity, showing an IC50 value of 1.47 ± 0.07 mg/mL in 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging assays. The alkaline protease extract from the intestine of M. mustelus produced hydrolysate with the highest angiotensin I-converting enzyme (ACE) inhibitory activity (82 ± 1.52% at 2 mg/mL). All the protein hydrolysates showed excellent solubility and interfacial properties that were governed by pH. The major amino acids detected in SHPHs were glutamic acid/glutamine, aspartic acid/asparagine, histidine and arginine, followed by methionine, phenylalanine, serine, valine and leucine. Overall, the results indicated that smooth hound by-products can be used to generate high value-added products, thus offering a valuable source of bioactive peptides for application in wide range of biotechnological and functional food applications.

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“…1 In preliminary experiments, this protein showed the unusual property of folding more rapidly in the presence of moderate concentrations of denaturant than it does in water. SFA-8 is known to form highly stable emulsions with oil/water mixtures (33), implying the presence of a large exposed surface of hydrophobic residues (34,35). Proteins generally shield hydrophobic groups from aqueous solution (1).…”

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Direct Kinetic Evidence for Folding via a Highly Compact, Misfolded State

Pandya

Williams

Dempsey

et al. 1999

Journal of Biological Chemistry

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The 2 S seed storage protein, sunflower albumin 8 (SFA-8), contains an unusually high proportion of hydrophobic residues including 16 methionines (some of which may form a surface hydrophobic patch) in a disulfide cross-linked, ␣-helical structure. Circular dichroism and fluorescence spectroscopy show that SFA-8 is highly stable to denaturation by heating or chaotropic agents, the latter resulting in a reversible two-state unfolding transition. The physical properties that direct a protein to its native fold are the subject of extensive experimental and theoretical investigation. It is generally accepted that the main driving forces in protein folding are formation of a distinct hydrophobic core by clustering of nonpolar groups (1) and local ordering of the backbone into elements of secondary structure according to the intrinsic properties of the amino acid residues and the need for pairing of backbone amide groups (2). The temporal development of these types of interaction, however, is more open to question. Hierarchic models of protein folding propose an initial formation of marginally stable local microdomains in which the secondary structure is well ordered, followed by their consolidation through the formation of longer sequence-range interactions and tertiary packing (3, 4). An alternative model suggests that global hydrophobic collapse drives an overall condensation of the polypeptide chain in the early stages of protein folding, which reduces the conformational possibilities and leads to the formation of secondary structure (5, 6).Experimental studies of the nature of states arising in the folding reaction have led to starkly divergent conclusions. It is undeniable that collapsed intermediate states accumulate transiently during the refolding of most globular proteins, particularly those with polypeptide chains of less than 100 residues (7). These compact intermediates are formed rapidly (microsecond time scale) (8, 9) and contain extensive secondary structure, but they lack the fixed and near crystalline tertiary side-chain contacts characteristic of the native conformation. These intermediates may be viewed as productive "on-pathway" states that guide the protein to its native fold through organizing the backbone topology (7, 10) or as nonproductive "off-pathway" states, which are kinetically trapped because the rate-limiting energy barrier that divides them from the native state is raised (11,12). In support of this latter view, lattice model simulations of heteropolymer organization suggest that partially folded intermediates contain stable, nonnative contacts that must be broken before the native structure is reached (13,14).Quantitative kinetic analyses of several proteins have been used to estimate the stability of such intermediates but do not determine whether these intermediates are productive or not (15)(16)(17)(18). Late folding intermediates with nonnative interactions have been observed experimentally and can be explained by incorrect proline isomers in the case of ribonuclease A (19) and r...

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Relationship of Composition to Protein Functionality

Cited by 26 publications

References 19 publications

Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates

Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates

Valorisation of smooth hound (Mustelus mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides

Direct Kinetic Evidence for Folding via a Highly Compact, Misfolded State

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