Physicochemical properties of proteins: Texturization via gelation, glass and film formation

Kinsella, John E.; Rector, D.; Phillips, Lance G.

doi:10.1007/978-1-4615-2670-4_1

Cited by 30 publications

(29 citation statements)

References 28 publications

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“…It has been noted that disulfide bonds reduce the flexibility of a protein. In the case of soy protein, the disulfide bonds not only limited molecular flexibility but also restricted foaming (Kinsella et al. 1994).…”

Section: Resultsmentioning

confidence: 99%

EFFECT OF NaCl ON GELATION CHARACTERISTICS OF ACID- AND ALKALI-TREATED PACIFIC WHITING FISH PROTEIN ISOLATES

Thawornchinsombut

Park²

2007

J Food Biochemistry

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The physicochemical properties of gels prepared from Pacific whiting protein isolated at pH 3 and 11 with three concentrations of NaCl were characterized after a pH readjustment to 7.0. The strongest gels were obtained from fish protein isolate (FPI) prepared at pH 11/150‐mM NaCl and conventional surimi. The protein solubilities of FPI treatments did not contribute significantly to their gel properties. Surface hydrophobicity and differential scanning calorimetry demonstrated that, in addition to adjusting the pH to 3 or 11, salt addition during protein solubilization and subsequent recovery at the isoelectric point (pI) led to protein denaturation. Rheological study indicated that gelation mechanisms of FPI were identical with the same NaCl concentration regardless of pH. The FPI prepared at pH 3 or 11 with NaCl could be partly refolded at pH 7. Nevertheless, some myosin fragments and actin did not refold. PRACTICAL APPLICATIONS Fish protein isolate (FPI) processing is a new concept for protein recovery using a pH shift. While conventional surimi processing is performed by avoiding protein denaturation, this FPI process is performed chemically by unfolding proteins and subsequent refolding. Since FPI is made with the inclusion of sarcoplasmic proteins, which are removed at the conventional surimi process, it guarantees a significant yield increase. This study revealed that the strongest gels were made from conventional surimi and FPI prepared at pH 11 and 15‐mM NaCl. It also confirmed that protein solubility does not support thegelation properties of FPI. Refolding of FPI prepared at extreme pHs (3 or 11) was noted, but in a full scale.

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Section: Resultsmentioning

confidence: 99%

EFFECT OF NaCl ON GELATION CHARACTERISTICS OF ACID- AND ALKALI-TREATED PACIFIC WHITING FISH PROTEIN ISOLATES

Thawornchinsombut

Park²

2007

J Food Biochemistry

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“…It was important that the rate of the second step remains slower than the first one, because protein aggregation will then be ordered enough to allow gel formation (Kinsella et al, 1994).…”

Section: Massagingmentioning

confidence: 99%

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Reddy¹,

Mandal²,

Sen³

et al. 2014

International J. of Meat Science

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To provide the consumer with a highly palatable product at a reasonable cost is the main objective of any food industry. Particular to meat industry, utilization of less valuable carcasses and carcass cuts and carcass components (plates, flanks, shanks, etc.) is of prime interest in periods of economic pressure. One such relevantly new technological approach is restructuring technology, which enables the production of value-added meat products from low value cuts and trimmings of carcasses. Although the economics and processing of restructuring meats appear favourable to producing a product that has the palatability attributes that are between an intact muscle steak and ground meat. This review of restructured meat products discuss the actual science and technology behind the restructuring of muscles, how muscle chunks are binding each together at protein molecules stage, factors influencing the meat pieces binding, type of restructuring methodologies, quality attributes of restructured meat products, problems of oxidation, use of natural antioxidants and recommends research needs for the future.

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“…The presence of intramolecular disulfide bonds restricts protein unfolding which is necessary to enable polypeptide chains to associate non-covalently into protein aggregates during heating. 16,17 Similarly, intermolecular disulfide bonds could prevent effective interactions between different polypeptide chains. The present result is similar to a previous report which showed that soybean β-conglycinin which does not have disulfide bonds was more susceptible to heatinduced coagulation than the glycinin fraction which contains disulfide bonds.…”

Section: Protein Content and Functional Propertiesmentioning

confidence: 99%

Comparative study of the polypeptide profiles and functional properties of Sinapis alba and Brassica juncea seed meals and protein concentrates

2005

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Defatted meals and protein concentrates from six accessions of Sinapis alba and one accession of Brassica juncea mustard seeds were analysed for their polypeptide profile and functional properties. Two types of protein concentrates were prepared using acid-induced and calcium-induced protein precipitations. Meals from the S alba seeds had similar polypeptide composition, which was different from that of the B juncea meal. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that two of the major polypeptides (50 and 55 kDa) in S alba seeds were susceptible to acid-induced precipitation but resistant to calcium-induced precipitation. The B juncea meal proteins were significantly (p ≤ 0.05) more susceptible to heat coagulation than the S alba meal proteins. Emulsifying activity index was significantly higher (p ≤ 0.05) in the B juncea meal and protein concentrates when compared with similar products from S alba. It was concluded that the presence of a high-molecular-weight (135 kDa) disulfide-bonded polypeptide could have contributed to the lower emulsifying power of the S alba products when compared with the B juncea proteins that do not have this polypeptide.

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Physicochemical properties of proteins: Texturization via gelation, glass and film formation

Cited by 30 publications

References 28 publications

EFFECT OF NaCl ON GELATION CHARACTERISTICS OF ACID- AND ALKALI-TREATED PACIFIC WHITING FISH PROTEIN ISOLATES

EFFECT OF NaCl ON GELATION CHARACTERISTICS OF ACID- AND ALKALI-TREATED PACIFIC WHITING FISH PROTEIN ISOLATES

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Comparative study of the polypeptide profiles and functional properties of Sinapis alba and Brassica juncea seed meals and protein concentrates

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