1,5-glucono-δ-lactone-induced gelation of myofibrillar protein at chilled temperatures

Ngapo, T.M.; Wilkinson, B. H. P.; Chong, R.

doi:10.1016/0309-1740(95)00028-3

Cited by 34 publications

(31 citation statements)

References 6 publications

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“…Calcium ions were the most important factor in SA gel formation; thereby CC had a highly significant effect on cold-set MP gelation. GdL itself has a potential to form a MP gel (Ngapo et al, 1996), but the GdL effects on MP gelation were not observed at low salt concentration (0.1 M) in this study. Consequently, the…”

Section: Calcium Alginate (Ca) Systemcontrasting

confidence: 62%

Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

Hong¹,

Chin²

2009

Korean Journal for Food Science of Animal Resources

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The aim of this study was to model and optimize the calcium alginate (CA) and microbial transglutaminase (TG) systems to form a cold-set myofibrillar protein (MP) gel containing 0.1 M or 0.3 M NaCl using a response surface methodology. The gel strengths of cold-set and heat-induced MP gels, and cooking yields were measured. All measured parameters showed determination coefficients (R 2 ) above 0.7 without a lack-of-fit. The CA system had the best results with component ratios of 1.0:0.3:1.0 corresponding to sodium alginate, calcium carbonate and glucono-δ-lactone, respectively, and was favourable at 0.1 M NaCl. In contrast, the TG system only had an effect on cold-set MP gelation at 0.3 M salt, and the optimal ratio of TG to sodium caseinate was 0.6:0.5. By combining the two systems at 0.3 M NaCl, an acceptable cold-set MP gel with an improved texture and high cooking yield could be formed. Therefore, these results indicated that the functionality of the cold-set MP gel could be enhanced by combining these two optimized gelling system.

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Section: Calcium Alginate (Ca) Systemcontrasting

confidence: 62%

Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

Hong¹,

Chin²

2009

Korean Journal for Food Science of Animal Resources

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“…All binder treatments resulted in a higher pH than that of the control (p<0.05), with the exception of CS treatment. Nevertheless, variations in pH between treatments were small (<0.04 pH unit), and the final pH of restructured pork might be mainly influenced by the addition of GdL (Ngapo et al, 1996). It should be noted that pressurization increases the pH of the meat (Hong et al, 2008).…”

Section: Resultsmentioning

confidence: 99%

“…Protein oxidation also enables cross-linking of proteins, thereby forming an irreversible polymer; however, the oxidative process coincides precisely with functional and nutritional losses of proteins (Xiong, 2000). Ngapo et al (1996) reported that a cold-set MP gel could be obtained by glucono-δ-lactone (GdL)-induced slow acidification.…”

Section: Introductionmentioning

confidence: 99%

Effects of Non-meat Protein Binders and Acidification on the Efficiency of Cold-Set Pork Restructuring by High Pressure

Hong¹,

Chun²,

Lee³

et al. 2012

Korean Journal for Food Science of Animal Resources

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We investigated the effects of non-meat protein binders combined with glucono-δ-lactone (GdL) on the binding properties regarding restructured pork prepared by high-pressure treatment. Soy protein isolate (SPI), casein (CS), whey protein concentrate (WPC), and egg white (EW) were used as non-meat protein binders and compared with the control (no binder) and with the κ-carrageenan (KC) treatment. The compression and depression rates were 2.3 and 37 MPa/s, respectively, and pressurization was conducted at 200 MPa for 30 min at 4 o C. After pressurization, the physical properties (pH, water-holding capacity, color, tensile strength, and microscopic structure) of the sample were evaluated. The combination of pressurization with acidification enabled cold-set meat binding, and the binding strength of restructured pork was enhanced by the addition of non-meat proteins. Among binders, SPI demonstrated the best efficiency in binding meat pieces. Therefore, the present study demonstrated that the combination of acidification and pressurization processes with the utilization of non-meat protein binders has a potential benefit in meat restructuring.

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“…It is generally recognized that the activation of both CA and TG systems depends on the pH (Sakamoto et al, 1994; Mancini et al, 1999). For the CA system, GdL has the potential to slowly reduce the pH via acid hydrolysis (Ngapo et al, 1996), which results in the slow release of Ca 2+ from CC (Draget et al, 1991).…”

Section: Results and Discussion Phmentioning

confidence: 99%

Evaluation of Salt, Microbial Transglutaminase and Calcium Alginate on Protein Solubility and Gel Characteristics of Porcine Myofibrillar Protein

Hong¹,

Chin²

2010

Korean Journal for Food Science of Animal Resources

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Response surface methodology was adopted to model and optimize the effects of microbial transglutaminase (TG) and calcium alginate (CA) systems of various ratios on the gelation characteristics of porcine myofibrillar protein (MP) at various salt levels. The CA system consisting of sodium alginate (SA), calcium carbonate (CC) and glucono-δ-lactone (GdL) showed no remarkable changes in the salt-soluble fraction, and only minor effects on electrostatic interactions were observed. Increasing CA concentration caused acid-induced hydrophobic interactions in MPs, resulting in increased MP gel strength. The TG system, containing TG and sodium caseinate (SC), induced cold-set MP gelation by formation of covalent bonding. The main advantage of the combined system was a higher cooking yield when the MP gel was heated. These results indicated that 0.7% TG combined with 0.8% CA system can form a viscoelastic MP gel, regardless of salt levels.

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1,5-glucono-δ-lactone-induced gelation of myofibrillar protein at chilled temperatures

Cited by 34 publications

References 6 publications

Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

Effects of Non-meat Protein Binders and Acidification on the Efficiency of Cold-Set Pork Restructuring by High Pressure

Evaluation of Salt, Microbial Transglutaminase and Calcium Alginate on Protein Solubility and Gel Characteristics of Porcine Myofibrillar Protein

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