Effects of Transgluninase and GDL on Gel Properties of Chicken Myofibrillar Proteins

Kun Sheng Zhang; Yun Xia Ren; Na Liu; Yong Qing Tao

doi:10.4028/www.scientific.net/AMR.554-556.1148

Paper Titles

Chemical Composition of Essential Oil from Fruit of Ficus Altissima
p.1125

Correlation Analysis between Biomass and Extracellular Alpha-Galactosidase Activity of Pediococcus acidilactici XS1B
p.1129

Effect of Staphylococcus xylosus and Lactobacillus fermentum Inoculation on Raw Pork Batters and Optimization of the Fermentation Conditions
p.1133

Anti-Proliferative Activity of Glycoprotein PLG-3 from the Submerged Mycelia of Phellinus linteus AML1101 In Vitro
p.1140

Effects of Transgluninase and GDL on Gel Properties of Chicken Myofibrillar Proteins
p.1148

Deproteinization of Polysaccharide from the Stigma Maydis by Chitosan Method
p.1152

Food Processing Technology Selection Method Based on Relative Membership Degree and Gray Incidence Analysis
p.1156

Quality Attributes of Four Major Retails Cuts from Songjiang Cattle
p.1160

Ultra High-Pressure and Ion Implantation Combined Mutagenesis to Improve the Production of β-Carotene from Red Yeast
p.1165

HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 554-556Effects of Transgluninase and GDL on Gel...

Effects of Transgluninase and GDL on Gel Properties of Chicken Myofibrillar Proteins

Abstract:

Myofibrillar protein gel properties were studied. Based on which Box-Benhnken center-united experiment was designed for optimization of ratio scheme for gelation strength. The optimum conditions for best gel strength were found to the transgluninase 0.37% of myofibrillar proteins, GDL 1.19%, in 0.88mol/L NaCl concentration at pH 5.96 to form 40mg/ml protein concentration solution. The gel strength was 316.953g. The study showed that transgluninase and GDL could interact significantly in improving gel strength (P <0.01).

You might also be interested in these eBooks

View Preview

Info:

Periodical:

Advanced Materials Research (Volumes 554-556)

Pages:

1148-1151

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.554-556.1148

Citation:

Cite this paper

Online since:

July 2012

Authors:

Kun Sheng Zhang, Yun Xia Ren, Na Liu, Yong Qing Tao

Keywords:

Gdl, Gel Strength, Myofibrillar Protein, Transgluninase

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

Citation:

References

[1] Zhu Y, Rinzema A, &Tramper J. Microbial transglutaminase-a review of its production and application to food processing. Appl. Microbial. Biotech. 44(1995), 277-282.

DOI: 10.1007/bf00169916

Google Scholar

[2] Yue, Zhen-Feng, &Wu-Hui. The application of D-glucose-delta-lactone in the food industry. Food Science and Technology, 6(1998), 32-33.

Google Scholar

[3] Donkeun Park, & Youling L. Xiong. Oxidative modification of amino acids in porcine myofibrillar protein isolates exposed to three oxidizing systems. Food Chemistry. 103(2007), 607-616.

DOI: 10.1016/j.foodchem.2006.09.004

Google Scholar

[4] Tomasz Lesiow, &Youling L. Xiong. Chicken muscle homogenate gelation properties: effect of pH and muscle fiber type. Meat science. 64(2003), 399-403.

DOI: 10.1016/s0309-1740(02)00206-1

Google Scholar

[5] Koo B. Chin , Mi Y. Go, & Youling L. Xiong. Effect of soy protein subsititution for sodium caseinate on the transglutanminate-induced cold and thermal gelation of myofibrillar protein. Food Research International, 42(2009), 941-948.

DOI: 10.1016/j.foodres.2009.05.008

Google Scholar