Casein micelles: structure, properties and enzymatic coagulation

Ruettimann, K.W.; Ladisch, Michael R.

doi:10.1016/0141-0229(87)90109-8

Cited by 46 publications

(23 citation statements)

References 57 publications

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“…In addition, milkfat globule size and concentration have shown large FIBER OFMC SENSOR RESPONSE TO MILKFAT 165 effects on absorption measurements (Ben-Gera and Noms 1968). The average particle diameter of casein micelles falls in the range of 130 to 160 nm (Ruettimann and Ladisch 1987) and milkfat in the form of globules in the range of 0.1 to 1.5 pm.…”

Section: Milk Propertiesmentioning

confidence: 99%

Fiber Optic Sensor Response to Low Levels of Fat in Skim Milk

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Payne

Hicks

et al. 2000

J Food Process Engineering

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A fiber optic transmission technique using single fibers to deliver and receive light was investigated for measuring the m'llcfat content of homogenized skim milk. Light transmission through skim milk for wavelengths of 400 to loo0 nm was measured using a fiber optic spectrophotorneter. Transmission was measured for distances of 0.5, I , 2, 3, 4 and 5 mm and for milk containing 0.05 to 0.21 wt% millcfat. Skim milk was centrifiged, and the resulting fractions mixed to yield samples with 5 diflerent milvat levels. Three optical responses were tested for correlation with miwat content. One used a light intensity measurement at a single transmission distance of 4 mm, the second used the light intensity ratio of two wavelengths at a single transmission distance of 4 mm, and the third used six different transmission distances to determine a light extinction coefficient at a single wavelength. The calibration equationsfrom all three methods were able to predict sample millcfat content with a RMSE of 0.008 to 0.01 2 wt % . Statistical analysis did not find a significant diflerence between the three methods. Hence, for simplicity using a single transmission distance is attractive for further sensor design.

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Section: Milk Propertiesmentioning

confidence: 99%

Fiber Optic Sensor Response to Low Levels of Fat in Skim Milk

Crofcheck

Payne

Hicks

et al. 2000

J Food Process Engineering

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“…To induce precipitation, about 90% of the j-casein chains needs to be cleaved. 16 The aspartic protease chymosin has its highest activity at pH 3-4 and it is the only enzyme known to specifically cleave the Phe 105 -Met 106 peptide bond in j-casein, resulting in separation of j-casein. 17,18 This process is commonly used in cheesemaking.…”

Section: Introductionmentioning

confidence: 99%

The enzyme-mediated autodeposition of casein: effect of enzyme immobilization on deposition of protein structures

2016

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The enzyme-mediated autodeposition on the example of casein is reviewed, and deposition of casein structures is investigated in relation to applied immobilization methods of enzyme. First, casein is described in detail with respect to its structure in aqueous environments, followed by presentation of historical and current nonfood applications of casein. The presented process uses enzymes to trigger deposition of bio-based particles in close proximity to a support surface and allows for a high control over film formation and site-specificity. This is ensured by immobilization of enzyme on the support material. The herein described system is based on casein as protein and chymosin as enzyme. Different immobilization methods are investigated with respect to obtainable casein coatings, layers, and structures. Physical adsorption of enzyme enables the formation of casein coatings with controllable film thickness and is suitable for in situ buildup of adhesive layers due to diffusion of enzyme. The highest control over film formation is provided by covalent attachment of enzyme. Based on the attained results, the enzymemediated autodeposition gives new insights into biological material design. Graphical abstractEnzyme Casein micelle intact Bulk zone (no enzyme) Reaction zone Phe Met Support Support Casein micelle cleaved

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“…Since many of the technologically important properties of milk, e.g., its white colour, stability to heat or ethanol and coagulation by rennet, are due to the properties of the casein micelles, there has been an economic and technological incentive to characterize their properties and elucidate their structure. An extensive literature on these subjects has accumulated and has been reviewed at regular intervals (e.g., de Kruif, 1998de Kruif, , 1999de Kruif & Holt, 2003;Farrell, 1973;Farrell & Thompson, 1974;Fox, 2003;Fox & Kelly, 2004;Garnier, 1973;Garnier & Ribadeau-Dumas, 1970;Holt, 1992Holt, , 1994Holt & Horne, 1996;Horne, 1998Horne, , 2002McMahon & Brown, 1984;McMahon & McManus, 1998;Morr, 1967;Payens, 1966Payens, , 1979Payens, , 1982Rollema, 1992;Rose, 1969;Ruettimann & Ladisch, 1987;Schmidt, 1980Schmidt, , 1982Slattery, 1976;Slattery & Evard, 1973;Tuinier & de Kruif, 2002;Visser, 1992;Walstra, 1990Walstra, , 1999Walstra, Geurts, Noomen, Jellma, & van Boekel, 1999;Walstra & Jenness, 1984;Waugh, 1971).…”

mentioning

confidence: 98%