Solubility of Cod Muscle Myofibrillar Proteins at Alkaline pH

Dagher, Shawky M.; Hultin, Herbert O.; Liang, Yong

doi:10.1300/j030v09n04_06

Cited by 13 publications

(11 citation statements)

References 13 publications

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“…The addition of HCl or NaOH solutions in order to change the pH values increased ionic strength. Between the certain points of ionic strength, 0.3–1.0 M sodium chloride 9 or 0.1–0.9 M salt, 10 the salting‐in effect was observed. As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

New approaches for the effective recovery of fish proteins and their physicochemical characteristics

2003

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Pacific whiting protein solubility was significantly affected as the pH shifted away from the isoelectric point (pH 5.5). The highest breaking force of gels was measured for fish proteins treated at pH 11, while high deformation values were obtained at pH 2 and 11. Sodium dodecylsulfatepolyacrylamide gel electrophoresis revealed that fish proteins were highly degraded by acid or alkali treatment. High activity of cathepsin B-like enzyme was detected from acid-aided fish proteins. Strong cathepsin L-like activity was found in fish proteins treated at pH 10.5, corresponding well to the lower breaking force and deformation. Disulfide bonds were thought to contribute to the high texture value of fish proteins treated at pH 11.KEY WORDS: acid-aided processing, alkali-aided processing, fish proteins, pH.

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Section: Resultsmentioning

confidence: 99%

New approaches for the effective recovery of fish proteins and their physicochemical characteristics

2003

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“…This may be due to the low dilution factor used during the homogenization step. Previous studies suggested that dilution factor is an important factor affecting protein solubility, and that a dilution factor of 36 or greater increases protein recovery yield . In this study a dilution factor of 6 was applied in order to be able to directly compare results to previously obtained results from the same laboratory.…”

Section: Resultsmentioning

confidence: 99%

Calcium hydroxide as a processing base in alkali‐aided pH‐shift protein recovery process

2016

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“…1996; Feng and Hultin 1997). The study of Dagher et al. (2000) also indicated that at low ionic strength (10 mM), the solubility of cod muscle proteins increased considerably between pH 8.9 and 9.2.…”

Section: Introductionmentioning

confidence: 91%

Role of Ionic Strength in Biochemical Properties of Soluble Fish Proteins Isolated From Cryoprotected Pacific Whiting Mince

Thawornchinsombut

Park

2005

Journal of Food Biochemistry

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Biochemical characteristics of Pacific whiting muscle proteins extracted at acidic, neutral and alkaline conditions were investigated as affected by various ionic strength levels. The protein solubility at pH 4 declined, as NaCl was added up to 200 mM, due to protein aggregation through hydrophobic interactions. In contrast, at pH 7 and 10, solubility increased as NaCl was added up to 400 mM after which it remained constant. Changes in total SH content and Sowere highly related to the different molecular weight distributions of the soluble proteins. At pH 4, myosin heavy chain (MHC) was soluble as evidenced by the presence of MHC in the soluble fraction, even though degraded molecules were shown at IS 10–100 mM, and became completely insoluble at IS ≥ 150 mM. At pH 10, the density of the MHC band gradually increased as IS increased and the formation of high MW polymers was observed at IS ≥ 150 mM.

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Solubility of Cod Muscle Myofibrillar Proteins at Alkaline pH

Cited by 13 publications

References 13 publications

New approaches for the effective recovery of fish proteins and their physicochemical characteristics

New approaches for the effective recovery of fish proteins and their physicochemical characteristics

Calcium hydroxide as a processing base in alkali‐aided pH‐shift protein recovery process

Role of Ionic Strength in Biochemical Properties of Soluble Fish Proteins Isolated From Cryoprotected Pacific Whiting Mince

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