Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)

Mohan, M.; Ramachandran, Dhanya; Sankar, T.V.; Anandan, R.

doi:10.1016/j.procbio.2007.04.005

Cited by 46 publications

(35 citation statements)

References 38 publications

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“…The solubility on 0-600 mM KCl was however the same between pH-treated and native myosin. Results that were similar to those of Kristinsson (2001) were later also observed by Mohan et al (2007). In their study, the head group of mullet (Mugil cephalus) myosin was more affected by acidification and alkalization than the rod part.…”

Section: Protein Conformational Changes Taking Place During the Acid supporting

confidence: 83%

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

Nolsøe

Undeland

2008

Food Bioprocess Technol

211

151

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The acid and alkaline solubilization processes for isolating muscle protein from ground fish raw materials are investigated by scrutinizing the literature. Following an introduction to the processes, with some underlying chemistry, patents related to the acid and alkaline solubilization process are described together with previously patented methods for processing of protein isolates. Focus is then placed on comparing a range of factors important in fish muscle protein isolation between the acid and alkaline solubilization processes, and classic washing-based surimi technology. The factors addressed were: protein yield, gel quality, color, lipid reduction, lipid oxidation, microbial stability, and frozen storage stability. A long series of studies made with different fish/shellfish species have been used for this purpose. Certain results are summarized in table form (protein yields, gel strength, and whiteness), others only in text form. From this part of the review, it is obvious that the acid process often has certain advantages (e.g., protein yield) and the alkaline process other ones (gel strength, whiteness, lipid removal, lipid oxidation, and total microbial count). Thus, the choice of method depends on the application. It is clear that most species respond differently to acid and alkaline solubilization, which is why the two methods are initially compared. In a section about new processing attempts, the use of the acid and alkaline methodology for isolating proteins from whole fish/shellfish and fish by-products is reviewed together with attempts to recover waste water proteins and attempts to modify the process. Tentative uses of the new protein isolates, e.g., as coatings, protein brines, and emulsifiers are finally described together with some conclusions and future opportunities for the acid and alkaline processes.

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Section: Protein Conformational Changes Taking Place During the Acid supporting

confidence: 83%

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

Nolsøe

Undeland

2008

Food Bioprocess Technol

211

151

View full text Add to dashboard Cite

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“…These authors observed that under alkaline conditions, the SH content decreases with increasing pH, indicating that perhaps the thiol groups are more susceptible to oxidation at alkaline pH, resulting in the formation of disulfide bonds. Mohan et al (2007), in their study with muscle proteins from liza (Mugil cephalus), also found that the concentration of RSH decreased when the homogenate protein was subjected to alkaline conditions, and explain that one reason may be the formation of disulfide bonds. On the other hand, the SM and SPC have much TSH and RSH compared with their respective gels (GM and GPC, respectively).…”

Section: Resultsmentioning

confidence: 96%

A Jumbo Squid (Dosidicus gigas) Protein Concentrate Obtained by Alkaline Dissolution and Its Conformational Changes Evaluation

Tolano-Villaverde¹,

Ezquerra‐Brauer²,

Ocaño‐Higuera

et al. 2013

FSTR

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Jumbo squid (Dosidicus gigas) is an important fishery resource in Mexico. It is abundant, but with little or nothing added value, therefore is necessary to search alternatives of processing. Due to its muscle characteristics, the aim of this study was to obtain protein concentrates by means of alkaline-aided solubilization followed by isoelectric protein precipitation. A protein concentrate (PC) was obtained from jumbo squid, and then compared with unwashed mantle mince (M). Surface hydrophobicity of PC was lower than M. Zeta potential showed a major potential of aggregation for PC. The total and reactive sulfhydryls groups were higher in M, while in sol-gel transition a reduction of total sulfhydryl groups was noticed. Thermogravimetric analysis revealed that PC loses water more easily that M, while the rheological evaluation showed that M formed a more elastic gel. The gelling properties of PC and M are governed by the physicochemical properties of proteins, which are affected by processing conditions.

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“…Along with an increasing public awareness of marine resources and worldwide demand for fish and fish products, produced from underutilized fish species, as functional foods, which are inexpensive and nutritional with palatable sensory evaluation, many efforts have been made to produce fish protein ingredients such as surimi, minced fish and FPI from small underutilized fish species [1][2][3]. Surimi is the largest source of fish protein ingredients.…”

Section: Introductionmentioning

confidence: 99%

Comparison of functional properties and SDS-PAGE patterns between fish protein isolate and surimi produced from silver carp

Azadian

Moosavi‐Nasab

Abedi

2012

Eur Food Res Technol

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The purpose of this study was to investigate and compare the physicochemical properties of fish protein isolate (FPI) produced from silver carp (Hypophthalmichthys molitrix), which is a relatively cheap fish with low consumption in Fars (a state of Iran). In this research, proteins were isolated using pH shifts method. Results showed that in terms of production efficiency, protein recovery, lipid reduction and functional properties such as water-holding capacity, emulsifying capacity, foaming capacity and water absorption, FPI was better than conventional surimi. The treated samples at pH = 2.5 represented better functional properties relative to other samples. The electrophoretic patterns demonstrated that acidic pH led to vanish high molecular weight protein bands because these proteins were converted to low molecular weight proteins, whereas basic pH caused the formation of high molecular weight proteins relative to myosin heavy chain. It seems that in basic pH, the proteins were linked together after denaturation and then aggregated. Overall, the results showed that physicochemical qualitative properties of FPI were better than those of conventional surimi.

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Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)

Cited by 46 publications

References 38 publications

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

A Jumbo Squid (Dosidicus gigas) Protein Concentrate Obtained by Alkaline Dissolution and Its Conformational Changes Evaluation

Comparison of functional properties and SDS-PAGE patterns between fish protein isolate and surimi produced from silver carp

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