Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme

نویسندگان

  • Ahmed S. Eissa
  • Saad A. Khan
چکیده

The role of enzyme crosslinking in mediating formation of hydrophobic association in chemically denatured whey protein isolates (WPI) is examined. WPI samples denatured with dithiothreitol (DTT) and incubated at 50 8C with and without transglutaminase enzyme show dramatic differences in viscosity, with the viscosity of the sample exposed to enzyme being lower by several orders of magnitude than the sample without enzyme. Upon further exposure of both samples to sodium dodecyl sulfate (SDS) to eliminate hydrophobic interactions, we observe no change in the viscosity of the sample previously treated with enzyme, suggesting this sample to have minimal hydrophobic associations. In contrast, the sample without enzyme shows a dramatic drop in viscosity indicating it to have had substantial hydrophobic associations. A similar trend but to a lesser extent is observed at a higher WPI concentration. These results taken together suggest that the formation of enzyme catalyzed 3-(g-glutamyl)lysine bonds attenuates hydrophobic interactions through steric hindrance and formation of compact molecules that limits exposure of the hydrophobic moieties. q 2005 Elsevier Ltd. All rights reserved.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The effect of microbial transglutaminase enzyme on some physicochemical and sensory properties of goat’s whey cheese

The effect of the microbial transglutaminase (MTGase) enzyme treatment on some properties of whey cheese made from goat’s milk whey was studied; the results shows that the yield of whey cheese increased about 0.7 and 1.01% by using the concentration of 4 and 8U gm-1 whey protein respectively, the addition of MTGase for producing whey cheese caused a clear increase in hardness and the higher har...

متن کامل

Improving the rheological properties of 18% wheat flour as affected by transglutaminase enzyme

Enzymes are useful to modify wheat proteins to preserve the gas better and to correct the rheological properties of the dough of weak flour and bread. Gluten proteins are highly impacting the quality of various gluten-based products, and transglutaminases (TGs) leading to the strengthening, stability and constancy of the dough as well as the improvement of the volume, texture and storage time o...

متن کامل

Influence of heat and pH on structure and conformation of whey proteins

22 23 The aim of this study was to understand the fundamental interactions responsible for 24 aggregation of whey proteins (WPs) at pH 6 and 3 during heating at 140 oC for 30 s in the 25 presence of different acidulants. The conformational changes in the various heat-treated WP 26 dispersions were studied using chemical bond blockers and analysed using differential 27 scanning calorimeter therm...

متن کامل

Reduction in the antigenicity of whey proteins by heat treatment: a possible strategy for producing a hypoallergenic infant milk formula.

Residual antigenic protein in heat-denatured cow's milk whey and in two commercial infant milk formulas was determined using enzyme-linked immunosorbent assays specific for beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin, bovine IgG1 and alpha-casein. This immunochemical assessment of antigenicity was related to the capacity of the preparations to sensitize immunologically when fed ...

متن کامل

Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme.

Dynamic and steady shear rheology is used to examine the synthesis of low-pH (approximately 4) whey protein gels obtained through a two-step process. The first step involves cross-linking of whey proteins at pH 8 and 50 degrees C using transglutaminase enzyme, while the second step entails cold-set acidification of the resulting solution using glucono-delta-lactone (GDL) acid. During the first ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2006