Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein.

Wan, Liping.; Xiong, Youling L.; Decker, Eric A.

doi:10.1021/jf00036a008

Cited by 41 publications

(38 citation statements)

References 17 publications

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“…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).…”

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

Wang

Xiong

1998

Journal of Food Science

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“…; Wan et al . ) and could be explored in the further study. Jiang and Xiong () suggested that a 7‐h incubation with MTGase accentuated the gel‐strengthening effect by these SPI samples.…”

Section: Resultsmentioning

confidence: 99%

Microbial Transglutaminase Catalyzed the Cross-Linking of Myofibrillar/Soy Protein Isolate Mixtures

Han

et al. 2014

Journal of Food Processing and Preservation

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The effects of temperature and ionic strength on the cross‐linking of myofibrillar protein isolate (MPI)/soy protein isolates (SPI) catalyzed by microbial transglutaminase (MTGase) were studied. The SPI treated with MTGase formed a substantial amount of cross‐linking at temperatures ≥50C. All the SPI constituents except the basic subunits (B) of glycinin were cross‐linked and formed polymers. For MPI/SPI mixtures heated with MTGase, the actin band was gradually reduced within the temperature range from 20 to 90C. The addition of KCl gradually reduced the protein band changes and the myosin heavy chain and actin bands became less noticeable detected by the sodium dodecyl sulfate–polyacrylamide gel electrophoresis. The rheological results indicated that the treatment of MPI with MTGase significantly improved the elasticity of the MPI gels, irrespective of the incubation time. MTGase treatment significantly enhanced the gel properties of the mixed MPI/SPI protein gels. Practical Applications Myofibrillar proteins are the main contributors imparting textural attributes and functional properties to muscle foods. Defining the performance of myofibrillar proteins during heat‐induced gelation is beneficial in maintaining quality and developing processed meat products and processes. A better understanding of the gelation properties of protein (muscle and nonmuscle) in the presence or absence of microbial transglutaminase, would contribute to improving its industrial utilization and the quality of meat products.

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“…Washing removes a substantial portion of these prooxidants, and the incorporation of propyl gallate in the washing process can effectively block lipid oxidation by terminating free radical chain reactions. Previous studies (Wan et al, 1993;Xiong et al, 1993;Srinivasan et al, 1996) showed that propyl gallate was highly capable of inhibiting TBARS formation in BHS during short-term storage at refrigeration temperatures. Our results demonstrated that propyl gallate was also effective during long-term storage at sub-freezing temperatures.…”

Section: Results and Discussion Lipid Oxidationmentioning

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Chemical Stability of Antioxidant‐Washed Beef Heart Surimi During Frozen Storage

Wang

Xiong

Srinivasan

1997

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 (sucrose, sorbitol). Samples were stored at Ϫ15, Ϫ29, and Ϫ70ЊC for 0.2, 2, 4, 12, 26 and 52 wk to observe oxidative changes in lipids (TBARS and dienes) and proteins (sulfhydryl, carbonyl, surface hydrophobicity, and myosin ATPase). Lipid and protein oxidation was minimal at Ϫ70ЊC. The freezethaw process caused lipid and protein oxidation in control samples at Ϫ15 and Ϫ29ЊC. Oxidation increased rapidly after 4 wk. Propyl gallate inhibited lipid oxidation but was ineffective against protein changes. After 12 wk, cryoprotectants promoted lipid and protein oxidation in the absence of propyl gallate.

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Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein.

Cited by 41 publications

References 17 publications

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

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

Microbial Transglutaminase Catalyzed the Cross-Linking of Myofibrillar/Soy Protein Isolate Mixtures

Chemical Stability of Antioxidant‐Washed Beef Heart Surimi During Frozen Storage

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