Casein hydrolysate. II. Functional properties of peptides

Haque, Zahurul; Mozaffar, Zahid

doi:10.1016/s0268-005x(09)80125-2

Cited by 59 publications

(42 citation statements)

References 17 publications

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“…Tryptic hydrolysates of sodium caseinate displayed an increase in emulsion activity index values (EAI) at pH values above and below pH 4.0-5.0 with maximal increase in EAI at a DH of 8% (Chobert et al, 1988a). However, maximal increases in emulsion activity for tryptic hydrolysates of acid casein were observed at DH values corresponding to 2-4% (Haque and Mozaffar, 1992). Our results are, therefore, more in agreement with those of Haque and Mozaffar (1992).…”

Section: Resultssupporting

confidence: 80%

“…However, maximal increases in emulsion activity for tryptic hydrolysates of acid casein were observed at DH values corresponding to 2-4% (Haque and Mozaffar, 1992). Our results are, therefore, more in agreement with those of Haque and Mozaffar (1992). Differences in results may be due to several factors including specificity of the enzymes used, method of determining DH and the methodology to determine emulsification properties.…”

Section: Resultssupporting

confidence: 75%

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Functional Properties and Bitterness of Sodium Caseinate Hydrolysates Prepared with a Bacillus Proteinase

Slattery

Fitzgerald

1998

Journal of Food Science

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The functional and physicochemical characteristics, and bitterness were evaluated on sodium caseinate hydrolysates generated with a commercial Bacillus proteinase complex. At low degrees of hydrolysis (0.5 and 1.0% DH) the hydrolysates compared to the unhydrolyzed substrate had increased emulsion activity at pH 2 and 4. However, higher DH resulted in lower emulsion activities. At pH 8 and 10, the low DH hydrolysates displayed increased foam expansion and decreased foam drainage compared to the starting substrate. The Bacillus proteinase hydrolysates at higher DH had similar bitterness values to tryptic hydrolysates at equivalent DH. However, the Bacillus hydrolysate at 0.5% DH was less bitter (p<0.05) than the tryptic hydrolysate at the same DH.

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Section: Resultssupporting

confidence: 80%

Section: Resultssupporting

confidence: 75%

Functional Properties and Bitterness of Sodium Caseinate Hydrolysates Prepared with a Bacillus Proteinase

Slattery

Fitzgerald

1998

Journal of Food Science

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“…Generally, a lower DH protein compared to its native counterpart gave better emulsion abilities. [38][39][40][41][42] A more in-depth discussion on the effects of molecular weight on the surface activity of the same set of whey protein isolates examined here can be found in a previous study. [28] At the highest fat addition level of 1:10 P:F the HWP215 and HWP406 emulsions produced relatively smaller droplet sizes of about 0.6 to 0.7 mm.…”

Section: Droplet Sizementioning

confidence: 94%

Effects of Emulsification of Fat on the Surface Tension of Protein Solutions and Surface Properties of the Resultant Spray-Dried Particles

Howes

Adhikari

et al. 2013

Drying Technology

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To examine the effect of protein adsorption on the fat-water interface on the surface composition of spray-dried particles, whey, hydrolyzed whey, and soy protein isolate emulsions were prepared at three different protein to fat ratios of 1:1, 1:5, and 1:10 and spray dried. Non-hydrolyzed whey protein isolate (WPI) and the more hydrolyzed whey protein solutions at 20.2% degree of hydrolysis (DH) had significantly lower surface tension values with fat than without fat. The correlation between the reduction of surface tension value of an emulsion and the increase in protein surface composition of powder particles was observed for WPI and HWP406 but was not observed for the other protein isolate types. It was clear that the spray-dried emulsions had fat as the dominant component on the surface of the powder particles and that the amount of protein on the surface became severely depressed at higher fat addition levels. In terms of its powder morphology, the unique powder structures such as the indentations and folds usually found on the surface of protein containing powders were not evident because they were compromised by the presence of high surface fat. The powder with higher surface fat had more crumpled particle structures and dimpled surfaces.

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“…[21] 0.5 g of sample was added to 10 mL of soybean oil in a centrifuge tube, and mixed for 30 seconds in a vortex mixer in duplicate. The oil dispersion was centrifuged at 2800 × g for 30 min.…”

Section: Functional Propertiesmentioning

confidence: 99%

Functional Properties of Grass Carp (Ctenopharyngodon Idella), Nile Perch (Lates Niloticus) and Nile Tilapia (Oreochromis Niloticus) Skin Hydrolysates

Wasswa

Tang

2008

International Journal of Food Properties

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The influence of using an endo-peptidase (alcalase) on the functional properties of hydrolysis products from Nile perch, Grass carp, and Nile tilapia skin was studied. Reaction conditions were controlled at pH 8.25, 60°C, and the enzyme was added on the basis of standard activity units at an enzyme to substrate ratio of 1.7 g/100 g protein. The reaction was allowed to proceed for 85 min and enzyme was inactivated by heat. The soluble protein fractions were recovered and lyophilized. All freeze-dried fish skin hydrolysates powders had a light yellow color and contained up to 90% protein. Nitrogen solubility varied from 95.93 to 98.72% and was not significantly different at 5% probability level. The water and oil holding capacities of the skin hydrolysates were good in the range of 2.8 to 3.2 mL/g and 3.4 to 3.8 mL/g, respectively. Emulsification capacity varied from 11.3 to 21 mL/0.5 g with Nile perch skin hydrolysate having the highest score while Nile tilapia skin hydrolysate was the lowest. Grass carp skin hydrolysate was not able to form stable foam, unlike the Nile perch and Nile tilapia skin hydrolysate. Alcalase treated freshwater fish skin exhibited satisfactory functional properties hence may play an important role as an ingredient in the food and pharmaceutical industry.

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Casein hydrolysate. II. Functional properties of peptides

Cited by 59 publications

References 17 publications

Functional Properties and Bitterness of Sodium Caseinate Hydrolysates Prepared with a Bacillus Proteinase

Functional Properties and Bitterness of Sodium Caseinate Hydrolysates Prepared with a Bacillus Proteinase

Effects of Emulsification of Fat on the Surface Tension of Protein Solutions and Surface Properties of the Resultant Spray-Dried Particles

Functional Properties of Grass Carp (Ctenopharyngodon Idella), Nile Perch (Lates Niloticus) and Nile Tilapia (Oreochromis Niloticus) Skin Hydrolysates

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