Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Enzymatic production of a protein or polypeptide
Patent
1994-04-13
1996-01-23
Lilling, Herbert J.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Enzymatic production of a protein or polypeptide
435 42, 435222, 426 7, 426 18, 426 32, 426 33, 426 41, 426 43, 426 46, 426556, 426557, 530343, 530407, 530822, 530833, A23J 334, A23J 310, A23J 120
Patent
active
054864615
DESCRIPTION:
BRIEF SUMMARY
The invention comprises a casein hydrolyzate and a method for production of such casein hydrolyzate.
Casein hydrolyzates are mainly used as constitutents in baby food, and many different casein hydrolyzates and methods for production of casein hydrolyzates are known. In relation to casein hydrolyzates and methods for production thereof at least four aspects are important in order to generate the best possible result: 1) a high DH (Degree of Hydrolysis), which results in shorther peptides in the product and thus in a low allergenicity, 2) low content of free amino acids, which results in a low osmolality which is preferred when the product is incorporated in a diet, 3) low bitterness, and 4) high yield.
Many methods for production of a casein hydrolyzate with good organoleptic properties can be carried out with a low yield only. Stated more generally, it is difficult to obtain an optimal balance between the above indicated four aspects. Thus, it is the purpose of the invention to indicate a casein hydrolyzate and a method for production of such casein hydrolyzate with optimal properties, i.e. with a high DH, a low content of free amino acids, low bitterness and high yield.
Surprisingly, according to the invention it has been found that a certain combination of specified enzymes and a non-pH-stat hydrolysis provides a process for production of a casein hydrolyzate with an optimal balance between DH, free amino acids, bitterness and yield.
The casein hydrolyzate according to the invention does not contain any unhydrolyzed casein, and it is characterized by the fact that the casein hydrolyzate is completely soluble or almost completely soluble in an aqueous medium with a pH value in the pH range of 3.5-7.0, that it is of good organoleptic quality, that it contains peptides in relative amounts corresponding to the following MW distribution (MW is an abbreviation for molecular weight):
______________________________________ weight-%
______________________________________
MW > 5000 0-1
5000 > MW > 1500 15-35
1500 > MW > 500 40-60
500 > MW 15-35
______________________________________
molecular weight (Mn) is 400-650.
BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 shows the molecular weight distribution and the accumulated molecular weight distribution of the casein hydrolyzate produced as indicated in Example 1.
FIG. 2 shows the molecular weight distribution and the accumulated molecular weight distribution of the casein hydrolyzate produced as indicated in example 2.
FIG. 3 shows the molecular weight distribution and the accumulated molecular weight distribution of the casein hydrolyzate produced as indicated in example 3.
FIG. 4 shows the rate of hydrolysis of rennet casein with and without phosphate, produced as indicated in example 4.
FIG. 5 shows the molecular weight distribution and the accumulated molecular weight distribution of the casein hydrolyzate produced as indicated in example 6.
FIG. 6 shows the molecular weight distribution and the accumulated molecular weight distribution of the casein hydrolyzate produced as indicated in example 7.
The MW distribution of peptides in protein hydrolyzates is determined as follows.
The sample is diluted, filtered and injected into a liquid chromatographic system, operating in the Gel Permeation Chromatography (GPC) mode. this separation technique utilizes a liquid flow through a column filled with porous particles, having pores with a well-defined pore diameter. When a solution of peptides, having different molecular sizes passes through the column, the small peptides will be able to flow into the pores while the larger peptides will be excluded from the pores. Thus, the peptides in a solution will be separated according to molecular size (and molecular weight), as the larger peptides will be eluted faster from the column than the smaller peptides. A detector at the column outlet continously measures the effluent. The chromatographic system is calibrated by means of peptides with known molecular weight. series and operated at ambient
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patent: 4600588 (1986-06-01), Ernster
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patent: 5141757 (1992-08-01), Dac et al.
patent: 5314873 (1994-05-01), Tomita et al.
patent: 5356637 (1994-10-01), Loosen et al.
Harrington James J.
Lilling Herbert J.
Novo Nordisk A S
Zelson Steve T.
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