Salt, Cryoprotectants and Preheating Temperature Effects on Surimi‐like Material from Beef or Pork

Park, S.; Brewer, M.S.; McKeith, F. K.; Bechtel, Peter J.; Novakofski, J.

doi:10.1111/j.1365-2621.1996.tb12204.x

Cited by 30 publications

(16 citation statements)

References 30 publications

(32 reference statements)

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“…Salt also increases dissociation of actomyosin through physical cuts or tears of the muscle fibers during comminuting. The dissociated myosin participates in gel matrix formation and binds water (Park and others 1996). The greatest gelling effect of Pacific whiting surimi at neutral pH was obtained at 2.5% NaCl among the salt concentrations tested between 0% and 2.5% (Chung and others 1993).…”

Section: Resultsmentioning

confidence: 99%

“…In addition to covalent dipeptide (lysine and glutamic acid) linkages, which were initiated by endogenous transglutaminase, intermolecular hydrophobic interactions probably contributed to the low temperature setting reaction (Lanier 2000). Setting induces conformational changes in the protein molecules by localized exposure and subsequent interaction of hydrophobic amino acid residues, resulting in the formation of a stronger gel (Park and others 1996). The requirement of salt addition to surimi paste for inducing setting also supports the role of hydrophobic interactions because certain salts, such as sodium chloride, act with water molecules to strengthen the hydrophobic interactions between proteins (Lanier 2000).…”

Section: Resultsmentioning

confidence: 99%

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Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

Kim

Park

2008

Journal of Food Science

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Salt effect on gelling properties of fish protein isolate (FPI) prepared by acid- and alkali-aided extraction was investigated. Acid- or alkali-extracted FPI formed significantly better gel texture with 0% NaCl than with 3% NaCl. Texture properties of acid- or alkali-extracted FPI decreased as NaCl content increased, especially at 2% to 3% salt. Contrarily, salt significantly promoted texture qualities of conventional surimi gels. The effect was highlighted when they were subjected to low temperature setting. The myofibrillar proteins in FPI were not solubilized when NaCl was added, perhaps due to protein aggregation caused by acid or alkali extraction. FPI solubility, however, was not closely related to their texture properties. Cold setting did not promote texture properties of FPI gels as much as conventional surimi gels. Acid-extracted gels gave the best color properties.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

Kim

Park

2008

Journal of Food Science

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“…Modified procedure of Park, Brewer, McKeith, Bechtel, and Novakofski (1996) was followed. Jars of frozen mixed gels were tempered and 2 g of SSP/sugars (0, 4, 8, 12%, w/w; XOS, Tre, Sor, Suc) mixed gels were dissolved in 0.6 M NaCl/0.05 M sodium phosphate buffer (pH 7.0) with gentle stirring for 1 h at 4°C.…”

Section: Protein Solubilitymentioning

confidence: 99%

Effects of xylooligosaccharides and sugars on the functionality of porcine myofibrillar proteins during heating and frozen storage

Chou¹,

Lin

2010

Food Chemistry

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“…In fish surimi, cryoprotectants are usually added to protect the functionality of surimi protein (Lee, 1990). Park et al (1996) showed that addition of cryoprotectants prior to freezing had no protective effect on gel-forming ability of surimi-like materials prepared from beef or pork skeletal muscles. Other researchers (Park et al, 1993) have reported that cryoprotectants had marked positive effects on protein solubility and gelation properties of minced beef.…”

Section: Introductionmentioning

confidence: 99%

Functional Stability of Antioxidant‐washed, Cryoprotectant‐treated Beef Heart Surimi During Frozen Storage

Wang

Xiong

1998

Journal of Food Science

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Beef heart surimi was prepared in the presence or absence of propyl gallate and blended with or without cryoprotectants (sorbitol, sucrose) prior to frozen storage at Ϫ15Њ, Ϫ29Њ, and Ϫ70ЊC up to 52 wk. Protein solubility, gelling characteristics, water-holding capacity, cooking yield, and emulsifying properties decreased during storage at Ϫ15Њ and Ϫ29ЊC for control surimi (without cryoprotectants). Propyl gallate alone did not influence functionality changes. However, functional properties were largely protected by cryoprotectants as well as at Ϫ70ЊC independent of cryoprotectants. Thus, unless extremely low temperatures are used, beef heart surimi subjected to long-term cryogenic storage should be mixed with cryoprotectants and antioxidants to preserve functionality.the methods of Wan et al. (1993). The pellet of BHS was diluted to a protein concentration of 50 mg/mL with 0.6M NaCl, 50 mM sodium phosphate buffer (pH 6.0). The sol was set at 4ЊC for 18h to ensure maximal protein solubility prior to rheological measurements. A Model VOR rheometer (Bohlin Instruments, Inc., Cranbury, NJ) equipped with parallel plates (upper plate dia 3.0 cm) was used for dynamic rheological measurements during protein gelation. Protein gels were formed by heating the BHS sol from 20 to 73ЊC at 1ЊC/min, and the sample temperature during heating was verified with a thermocouple. The gelling samples were sheared at a fixed frequency (0.1 Hz) with a maximum strain of 0.02.To determine gel strength, gels were prepared by heating 5 g of the above BHS sol in glass vials (15 mm i.d. ϫ 65 mm l) from 20 to 75ЊC at 1ЊC/min in a water bath, followed by chilling in an ice slurry. After overnight setting at 4ЊC, gels, while still in the vials undisturbed, were equilibrated at room temperature (24ЊC) for 40 min and subsequently penetrated using a steel rod (12.5 mm dia with flat end) attached to the load cell (1 kg capacity) in a Model 4301 Instron universal testing machine (Instron Corp., Canton, MA). The crosshead speed was set at 20 mm/min. The force required to disrupt the gels (first peak) was used to represent gel strength. Cooking yield and water-holding capacityCooking yield and water-holding capacity (WHC) were determined as described by Daum-Thunberg et al. (1992). About 2 g aliquots of protein sol were weighed into glass vials (15 mm dia ϫ 40 mm l) and set at 4ЊC for 18h. The protein sol was cooked in a water bath at 1ЊC/min to 75ЊC. Cooked gels were chilled in an ice slurry and stored at 4ЊC for 18h. Gel weights were recorded after the vials were inverted and the cooked-out liquid was absorbed with a paper towel. Cooking yield was calculated as the weight of blotted gel divided by the weight of protein sol then multiplying by 100. Gels after the cooking yield determination were placed in thimbles folded with filter paper (2 pieces with a 5.5 cm dia at the outer layer and 1 piece with a 7.5 cm dia at the inner layer) and centrifuged at 30,000 ϫ g (Sorwall RC-5B, Du Pont Instruments, Fairview, TN, Rotor SS34 16,000 rpm) for 15 min. Afte...

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Salt, Cryoprotectants and Preheating Temperature Effects on Surimi‐like Material from Beef or Pork

Cited by 30 publications

References 30 publications

Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

Effects of xylooligosaccharides and sugars on the functionality of porcine myofibrillar proteins during heating and frozen storage

Functional Stability of Antioxidant‐washed, Cryoprotectant‐treated Beef Heart Surimi During Frozen Storage

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