CH620098A5 - Method for flavouring proteins - Google Patents

Abstract

Proteins are flavoured by treating them with an oil, a fat or a mixture of oil and fat in combination with an emulsifier, and by adding the flavour thereto subsequently or by treating them simultaneously with an oil, a fat or a mixture of oil and fat in combination with an emulsifier, and with the chosen flavour.

Description

620,098

2

CLAIM

Process for the flavoring of proteins, characterized in that:

a) said proteins are treated with an oil, a fat or a mixture of oil and fat in combination with an emulsifying agent and the flavor is then added; or b) said proteins are simultaneously treated using an oil, a fat or a mixture of oil and fat in combination with an emulsifying agent, and the selected flavor.

Food can be thought of as a complex mixture of proteins, fats, carbohydrates, water and other organic products. Meat, whether from mammals, birds or fish, for example, is one of the most common sources of foods with high protein content.

In populations experiencing strong demographic development, and more particularly in the so-called developing countries, meat and meat products are gradually being replaced by foods of essentially vegetable origin. Such a change in diet is not without greatly reducing the amount of protein consumed by the populations concerned, which causes a certain imbalance in food and can even lead to malnutrition or even undernourishment.

There is therefore a very serious need, which is constantly increasing, for meat substitutes with a high protein content, easily accessible as regards their price and moreover perfectly acceptable from the organoleptic point of view. This is the reason why the food industry constantly strives to develop meat substitutes.

Given their relatively low cost of production and their high nutritional value, proteins of plant origin, such as those of soya for example, or monocellular proteins, obtained for example from yeasts, constitute a material of choice for the confection bases or food additives for the preparation of meat substitutes.

One of the major obstacles to widespread consumption of soy proteins in human food is the relatively unpleasant taste and odor of such products, hence the need for the flavor industry to mask this unpleasant taste and to make organoleptically acceptable products prepared from soy.

It is known in the art that one of the problems encountered during the flavoring of food resides in the excessive absorption of the flavoring ingredients by some of the components of the food; the restitution of the aroma during the ingestion of the food is thereby altered, or even completely eliminated.

Little work has been done to date on protein flavoring. Some of them, however, have shown that the proportion of flavoring ingredient absorbed by proteins increases as a function of the hydrophobic nature of said proteins. It was postulated that high proportions of ingredient, retained in mass by hydrophobic interactions, were weakly linked, while small quantities could be comparatively more strongly linked, by polar interactions [Aroma Research, “Proc. Zeist Pudoc Symposium, Waeningen ”, p. 143-157]. Other studies have shown that the quantity of aldehydes and ketones absorbed by bovine serum albumin (“Bovine Serum Albumin”: BSA) and by Soyamine® 90 increases linearly with the concentration of the ligand [Beyeler, “ Aromatisierung von Proteinreichen Lebensmitteln ”, diss. No. 5275, EPF Zurich (1974)].

Finally, other studies have shown that the addition of an emulsifying agent to BSA or Soyamine 90 decreases the amount of benzaldehyde absorbed by such protein substrates [Studer, “Bindung von Aromastoffen an Sojaprotein und RSA in Gegenwart von Lipophilen, wasserlöslichen Verbindungen ”, Diplomarbeit, EPF Zurich (1974)]. However, such investigations do not provide any solution to the practical, industrial realization of protein flavoring.

We have now discovered that it is possible to reduce the quantity of flavor absorbed by a protein substrate, and thereby facilitate its restitution, when said substrate is treated with an oil, a fat or a mixture. of oil and grease, in combination with an emulsifying agent.

The subject of the invention is therefore a process for the flavoring of proteins, characterized in that:

a) said proteins are treated with an oil, a fat or a mixture of oil and fat in combination with an emulsifying agent and the flavor is then added; or b) said proteins are simultaneously treated using an oil or a mixture of oil and fat in combination with an emulsifying agent, and of the selected flavor.

The sources of vegetable proteins are very varied, the oil seeds being however most abundantly used for this purpose. Mention may be made, for example, of soybean, cotton, sunflower and sesame seeds, as well as peanuts and cereals such as wheat, corn, barley and oats, for example.

According to the invention, lipids are used in the form of oil, fat or mixtures of oil and fat. These are hydrophobic, solid or liquid products, represented by one of the following classes of compounds: fatty acids, mono-, di- and triglycerides, phospholipids, sterols, plasmagens and lipoproteins. Oils and fats of vegetable or animal origin should be used suitably. For practical and economic reasons, peanut, soybean or sunflower oils are preferably used.

According to the invention, emulsifiers are also used, in combination with the oils, fats or mixtures of oil and fat mentioned above. Such agents have the particular effect of facilitating the addition of the protein flavor or substrate when the latter is carried out in the presence of oil or fat. They can, for example, greatly increase the dispersion of proteins within the medium. They can also react with the protein substrate and modify the absorption properties of the aroma. Among the emulsifying agents which can be used according to the invention include lipids, proteins, polysaccharides, ionic or nonionic. A list of commercial emulsifiers will be given below, which can be favorably used in the context of the present invention.

Emulsifying agent

Commercial source

Artodan SP 30

Grinsted Products, A / S Grinstedvaerket,

8220 Braband, Denmark

BRIJ 35

Art. 801962, Merck Co., Darmstadt,

Germany

Egg yolk

Sigma Chem., C.P. 14508, St. Louis, MO.

83178, United States

Kraflow

Kraft Foods, Chicago, 111. 60690, USA

United

Leciflow

Kraft Foods, Chicago, 111. 60690,

United States

MO-33-F

Hefti AG, 8048 Zurich

Panodan AF

Grinsted Products, A / S Grinstedvaerket,

8220 Braband, Denmark

Panodan AM

Grinsted Products, A / S Grinstedvaerket,

8220 Braband, Denmark

RS-55-100

Hefti AG, 8048 Zurich

Sodium cholate

Art. 12448, Merck Co., Darmstadt,

Germany

5

10

15

20

25

30

35

40

45

50

55

60

65

3

620,098

Emulsifier Commercial source

Sodium deoxycholate

Sodium dodecyl hydrogen sulfate Span 20 Triton-X-100 Tween 20 Tween 40 Tween 60 Tween 80

Art. 6504, Merck Co., Darmstadt, Germany

Art. 2969, Merck Co., Darmstadt, Germany

Servo, Heidelberg, Germany Bender und Hobein AG, 8000 Zurich Serva, Heidelberg, Germany Serva, Heidelberg, Germany Serva, Heidelberg, Germany Serva, Heidelberg, Germany

According to a particular embodiment of the present invention, natural emulsions can be used as mixtures of oils or fats in combination with an emulsifying agent. For example, milk, uperized cream or various mixtures of cream and milk can be used as they appear on the market.

The amount of flavor, ingredient or composition to be added to proteins can vary widely and depends in particular on the desired flavoring effect. This amount also depends on the nature of the protein substrate as well as on the nature of the flavor component (s). However, it is within the competence of those skilled in the art to determine the concentration limits, which will vary according to the problem posed. Proportions of the order of 250 ppm relative to the weight of the finished product are suitable for the purpose sought and correspond to those used in general in the food industry.

The amounts of emulsifier to be added according to the invention also vary widely, concentrations ranging from

1 to 100, even 400% by weight of processed proteins which can be suitably used. The concentration limits will also be determined by the fact that the product thus treated must remain fit for consumption.

We have found that the absorption of the aroma, ingredient or composition, by the protein substrate decreases as a function of the lowering of the lipid content of natural emulsions (milk, cream, etc.). This absorption, on the other hand, remains more or less constant beyond a certain lipid level, which means that it therefore becomes unnecessary, and not very profitable from the economic point of view, to increase the proportion of lipids, oils or fats, above this limit rate.

The invention will be illustrated by means of the following example (temperatures in degrees centigrade).

Example

Benzyl alcohol, benzaldehyde and n-butanol were chosen as representative flavoring ingredients. The corresponding isotopes, labeled with 14C, can be obtained commercially (New England Nuclear, Boston, Mass. USA, or Radio-chemical Center, Amersham, Great Britain).

The buffer solution used (Soerensen, pH 7.4) was prepared from KH2PO4V15M and NaîHPO ^^ OVisM, according to "Documenta Geigy Wissenschaftliche Tabellen", p. 227.

The counting measurements were carried out using an Isocap 300 liquid scintillation counter (Nuclear, Chicago). The counts of the samples labeled with 14C were carried out in Rotiszint 22 (E. Roth, Karlsruhe, RFA).

Measurements carried out on flavoring ingredients (ligands) marked with UC (“shaking method”)

A) 1. Solutions of varying concentrations of unlabeled ligand are distributed in several containers.

2. Each of said solutions is then added with a small amount of ligand labeled with 14C.

3. A determined volume of each of the radioactive ligand solutions prepared above is then removed and subjected to a counting measurement: the relationship existing between the counts per minute (cpm) recorded and the concentration in ligand is thus established. .

B) 1. A determined quantity of protein (Soyamine® 90, Lucas Meyer, Hamburg, RFA) is first weighed in a 100 ml Erlenmeyer flask.

2. A portion of each of the radioactive ligand solutions 10 (see A2) is then added to the protein portion, so that the latter is in solution or suspension at 1%.

3. Once hermetically sealed, the containers are shaken mechanically for 16 h at room temperature.

4. From each of said containers, a portion is then collected of liquid, then subjected to centrifugation (12,500 rpm)

for 5 min and, from the supernatant, an aliquot is taken which will be subjected to counting. The quantity of ligand in solution is determined by means of the relationship established under figure A3.

20 The quantity of ligand (flavoring ingredient) linked to the protein (Cb) is then obtained by means of the formula

Cb = C0 — Q

wherein C0 represents the initial concentration of ligand and Cf the concentration of ligand in solution.

The protein used during the above experiment was prepared as follows: a suspension of 5 or 6% of Soyamine 90 in water is rapidly introduced into a dialysis tube (inside 7.8 cm) previously rinsed with distilled water. Impurities having a molecular weight of less than 10,000-15,000 are thus removed. Dialysis takes place for 3 days at 4 °, in the presence of distilled water. The protein in suspension is then centrifuged and finally lyophilized.

Measurements carried out in the presence of emulsifying agents

3s The ingredients used are benzaldehyde and n-butanol, labeled with 14C. The proteins used are Soyamine 90, bovine serum albumin (BSA) and denatured BSA, all in the form of a 1% suspension in the buffer according to Soerensen.

Various methods for the introduction of the emulsifying agent have been used: an aqueous suspension of lecithin (from egg yolks) has been added to hydrated Soyamine 90, so as to obtain a proportion of 1% of lecithin relative to the weight of protein. After being treated with ultrasound, the mixture was lyophilized and used as indicated previously for Soyamine 45 (“shaking method”).

Identical measurements were made from Soyamine 90 mixed at a rate of 1, 10% of Kraflow and BSA containing 10% of Kraflow, respectively, treated with ultrasound and lyophilized.

The emulsifier according to Grinsted was introduced as follows: dissolution in a minimum quantity of organic solvent, addition of water then addition of Soyamine 90 with stirring, treatment with ultrasound and finally lyophilization. The following agents were thus used (proportions):

Ardotan SP 30 (1 and 10%)

55 Panodan AM (10%)

Panodan AF (1%)

Mixtures of emulsifier and buffer previously treated with ultrasound were prepared for Brig 35, Tween 20 and for Sorbitan monooleate. Mixtures of variable concentrations 60 were then distributed in containers and brought to 45 ml: we thus obtained proportions of 1,100 and 400% in emulsifying agent relative to the protein. 5 ml of radioactive ligand solution were added to each portion and the measurements were carried out as indicated above.

65 The denatured BSA used above was prepared as follows: a 5% solution of crystallized BSA (Povite Production NV, Amsterdam, Holland) in the buffer according to Soerensen was brought to the isoelectric point (pH 4.4) by addition hydrochloric acid

620098

IN. After being heated with stirring for 1 day at 60 °, the protein precipitate was filtered and finally lyophilized.

Measurements made for variable lipid content

By combining various quantities of milk, cream and buffer according to Soerensen, emulsions with variable lipid content were obtained (see table).

Cream (ml)

Milk (ml)

Buffer (ml)

% of lipids1

0

0

25

0

0

5

20

0.63

0

10

15

1.27

5

0

20

2.50

0

25

0

3.17

10

0

15

5.00

10

15

0

6.90

15

0

10

7.50

15

10

0

8.77

20

5

0

10.63

25

0

0

12.50

1 For a total liquid phase of 30 ml.

The absorption of benzyl alcohol (3.3 10 ~ 2M in the lipid system above) on Soyamine 90 (1% of the total phase) was measured as a function of the increase in the lipid level. In this case, the method described above has been modified as follows: after centrifugation (12,500 rpm), the content of the test tubes is separated into three phases: a layer of fat, an intermediate liquid and a white precipitate mixed with Soyamine. After freezing in liquid nitrogen, the precipitate is eliminated and the measurement is carried out, after reheating on an emulsion prepared mechanically from the two remaining phases.

Measurements for a specific lipid content

Solutions of varying concentrations of ligand were prepared by adding benzyl alcohol to milk, so as to obtain concentrations varying from 1 × 10 −4 M to 2 × 10 −3 M. The counting measurements were then made as indicated above. ("Shaking method").

Measurements made for oil-buffer systems

The original shaking method has been modified as follows: 0.1 g of Soyamine 90 is weighed in 20 ml test tubes, 2 ml of oil are added (which will correspond to 16.7% of the total liquid phase), then the whole is stirred for 30 s using a vortex mixer. Then added 10 ml of a buffered solution of benzyl alcohol labeled with 14C and the mixture obtained is finally stirred for 16 h at room temperature.

The upper layer of oil is then quantitatively collected and subjected to centrifugation (5 min at 12,500 rpm) in order to be definitively rid of the traces of buffer which were still dispersed there. When the counting measurements are carried out on samples of identical volumes both of the oily phase and of the buffer solution, the quantity of ligand bound to the protein can be obtained by means of the following formula:

Cb = C0—0.2 (Oil) - Buffer where C0 represents the initial ligand concentration, Chuiie the concentration of the ligand in the oily phase and Cumpon the concentration of the ligand in the remaining buffered solution.

The effect of the addition of oil during the absorption of the ligand by the protein can then be determined by comparison of the value of Cb obtained above with that measured in the absence of oil.

Isothermal absorption measurements

For each of the ligands considered, the absorption on Soyamine 90 or denatured BSA is measured as a function of the initial ligand concentration.

Table I and fig. 1 relate to the absorption of n-butanol on denatured BSA (1% of the total phase). Table II and fig. 2 relate to the absorption of n-butanol on Soyamine 90 (1%). Table III and fig. 3 relate to the absorption of benzaldehyde on Soyamine 90 (1%). Table IV and fig. 4 relate to the absorption of benzyl alcohol on Soyamine 90.

In the latter case, the relationship between Cb and C0 does not appear to be linear, at least for initial ligand concentrations of less than 8 x 10 -4M.

Absorption measurements carried out in the presence of an emulsifying agent

As indicated previously, two distinct modes for the addition of the emulsifying agent were used: in the first case, the protein is mixed with the emulsifying agent, dried and then used as a pretreated substrate. Fig. 5 relates to measurements of ligand absorption in the presence of an emulsifier at 1 and 10% relative to the weight of protein. It can be seen that this mode of introduction does not substantially modify the absorption of the ligand by the protein.

In the second case, the ligand and the emulsifying agent are first mixed with the buffer solution, before being added with dried protein. Fig. 6 relates to measurements of absorption of benzyl alcohol on Soyamine 90 (1% of the total phase). It can be seen that the effect increases with the addition of the emulsifying agent (i.e., the amount of ingredient retained by the protein substrate decreases).

When the hydration of the protein is first carried out, then the addition of an emulsifying agent and finally treatment with ultrasound, the effect of said agent on the absorption of the flavoring ingredient is even more marked (see FIG. . 7, 8 and 9).

Absorption measurements carried out in the presence of natural emulsions

Fig. 10 relates to measurements of absorption of benzyl alcohol on Soyamine 90 (1%) as a function of the level of lipid present in the medium.

There is a rapid decrease in the amount of ligand retained by the protein substrate up to a lipid level of approximately 4%, very slow beyond this value.

Table V brings together measurements of absorption of benzyl alcohol on Soyamine 90, carried out in the presence of milk (lipid content: 3.8%) used in this case as a solvent. It can be seen that for high initial concentrations of ligand, the effects measured in milk are similar to those measured in buffer solution (Table IV).

However, for initial ligand concentrations of less than 2 × 10 −2M, the lowering of the absorption of the ligand on the protein is more marked than in the buffer solution.

This effect is particularly significant for a range of ligand concentrations as used in the flavoring of food (see fig. 11 and 4, respectively).

Absorption measurements carried out in the presence of edible oil

Fig. 12 relates to measurements of absorption of benzyl alcohol on Soyamine 90 (1%) carried out in the presence of a commercial edible oil, prepared from peanut oil and sunflower oil. Fig. 12 also includes similar measurements, carried out in the absence of oil.

It can be noted, by comparing the two curves obtained, that the addition of edible oil causes a reduction in the amount of ligand retained by the protein substrate.

Factors influencing the absorption of the ligand by the protein substrate

The results of the measurements described above indicate, for a given concentration range, that the absorption of the ligand

4

5

10

15

20

25

30

35

40

45

50

55

60

65

5

620098

(flavoring ingredient) depends on the nature and the protein concentration in the medium.

The absorption of the ligand depends on the level of lipid contained in the medium. The reduction in absorption is significant up to a lipid level of approximately 4%, very moderate beyond this value.

The absorption of the ligand can be modified significantly by the addition to the medium of natural emulsions such as milk or cream for example, at least for low initial concentrations of ligand.

Table I:

Absorption of n-butanol on denatured BSA

C0 M / L

CfM / L

Cb M / L

cb r

*%

c0

1 1.49 xlO "4

Q

4.0x10 "2

3.8482x10 "2

0.1518 x10 "2

10.1899

264.75

3.80

4.0 x 10 "2

3.8345

0.1655

11.1074

289.67

4.14

3.6x10 "2

3.4579

0.1421

9.5369

275.80

3.95

3.6x10 "2

3.4596

0.1404

9.4228

272.37

3.90

3.2x10 "2

3.0591

0.1409

9.4564

309.12

4.40

3.2x10-2

3.0685

0.1315

8.8255

287.62

4.11

2.8x10-2

2.6998

0.1002

6.7248

249.09

3.58

2.8x10 "2

2.6400

0.1600

10.7383

406.75

5.71

2.0x10 "2

1.9121

0.0879

5.8993

308.53

4.40

2.0 x 10 ~ 2

1.9139

0.0861

5.7785

301.92

4.31

1.6x10 "2

1.5085

0.0915

6.1409

407.09

5.72

1.6x10 "2

1.5130

0.0870

5.8389

385.92

5.44

1.2x10 "2

1.1402

0.0598

4.0134

351.99

4.98

1.2x10 "2

1.1436

0.0564

3.7852

330.99

4.70

8.0x10 "3

7.5577 xlO "3

0.4423x10 "3

2.9685

392.8

5.53

8.0x10 "3

7.5393

0.4607

3.0919

410.1

5.76

4.0x10 "3

3.8027

0.1973

1.3242

348.2

4.93

4.0x10 "3

3.7638

0.2362

1.5852

421.2

5.91

8.0 x 10 "4

7.4463 x 10 "4

0.5537 x10 "4

0.3716

499

6.92

8.0 x 10 "4

7.3577

0.6423

0.4311

586

8.03

For the meaning of the symbols, see Beyeler et al, Lebensmitt. Wiss. und Technol. 7, 313 (1974).

Table II:

Absorption of n-butanol on Soyamine 90

C „M / L

QM / L

Cb M / L

cb r

neither o

O I CT

r 2xl0 "4

Q

3.6 x 10 "2

3.4640 x 10 "2

0.1360 x10 "2

6.8003

196.31

3.78

3.6 x 10 "2

3.4296

0.1704

8.5210

248.45

4.73

2.8 x 10 "2

2.6604

0.1396

6.9785

262.31

4.99

2.8x10 "2

2.6648

0.1352

6.7612

253.72

4.83

2.0x10 "2

1.8862

0.1138

5.6885

301.58

5.69

2.0x10 "2

1.9010

0.0990

4.9481

260.29

4.95

1.6 x 10 "2

1.5356

0.0644

3.2187

209.61

4.03

1.6 x 10 "2

1.5213

0.0787

3.9332

258.54

4.92

1.2 x 10 "2

1.1269

0.0731

3.6525

324.12

6.09

1.2 x 10 "2

1.1192

0.0808

4.0405

361.02

6.73

8.0 x 10 "3

7.6637x10 "3

0.3363 xlO "3

1.6816

219.4

4.20

8.0x10 "3

7.6692

0.3308

1.6540

215.7

4.14

4.0 x 10 "

3.7782

0.2218

1.1092

293.6

5.55

4.0x10 "3

3.7874

0.2126

1.0632

280.7

5.32

8.0 x 10 "4

7.5280 x10 "4

0.4720 x10 "4

0.2360

314

5.90

8.0 x 10 "4

7.4001

0.5999

0.2999

405

7.50

620098

6

Table III

Benzaldehyde absorption on Soyamine 90

Co M / L

See M / L

Cb M / L

vs"

r—

r

£ *

2x 10 ~ 4

Q

2.0x10 "2

1.8202 x10 "2

0.1798 x 10 "2

8.9888

493.83

8.99

2.0 x 10 "2

1.7497

0.2503

12.5147

715.25

12.52

1.8 x 10 "2

1.6010

0.1990

9.9491

621.42

11.06

1.8 x IO "2

1.6002

0.1998

9.9893

624.25

11.10

1.4 x 10 "2

1.2555

0.1445

7.2243

575.41

10.22

1.4 x 10 ~ 2

1.2260

0.1740

8.6989

709.53

12.43

1.0 x IO "2

0.8835

0.1165

5.8271

659.58

11.65

1.0x10-2

0.8797

0.1203

6.0126

683.44

12.03

8.0 x 10 "3

7.0522 xlO "3

0.9478 x10 "3

4.7390

672.0

11.85

8.0 x 10 ~ 3

7.1281

0.8719

4.3593

611.6

10.90

6.0 xlO-3

5.2984

0.7016

3.5082

662.1

11.69

6.0x10 "3

5.2464

0.7536

3.7680

718.2

12.56

4.0x10 "3

3.4307

0.5693

2.8466

829.7

14.23

4.0 x 10 "

3.4055

0.5945

2.9725

872.9

14.86

2.0x10 "3

1.7501

0.2499

1.2493

713.8

12.50

2.0x10 "3

1.7878

0.2122

1.0609

593.4

10.61

8.0 x 10 "4

7.2681 x IO "4

0.7319 x 10 ~ 4

0.3659

503

9.15

8.0 x IO "4

7.0403

0.9597

0.4798

682

12.00

4.0 x 10 "4

3.5580

0.4420

0.2210

621

11.05

4.0 x 10 "4

3.5677

0.4323

0.2162

606

10.81

Table IV:

Absorption of benzyl alcohol on Soyamine 90

Point

C „M / L

See M / L

Cb M / L

cb r

1

O

X CS

1

Q

1

2.0 x 10 "1

1.8928 x 10 "1

0.1072 xlO "1

53.60

283.18

2

1.8

1.6969

0.1031

51.55

303.79

3

1.6

1.5189

0.0811

40.55

266.97

4

1.4

1.3142

0.0858

42.90

326.43

5

1.2

1.1307

0.0693

34.65

306.45

6

1.0

0.9539

0.0461

23.05

241.64

7

8.0 x 10 "2

7.5051 x 10 "2

0.4949 x10 "2

24.75

329.71

8

6.0

5.6668

0.3332

16.66

293.99

9

4.0

3.7292

0.2708

13.54

363.08

10

2.0

1.7055

0.2945

14.73

863.38

11

1.8

1.6891

0.1109

5.55

328.28

12

1.6

1.4549

0.1451

7.26

498.66

13

1.4

1.2583

0.1417

7.09

563.06

14

1.2

1.0607

0.1393

6.97

656.64

15

1.0

0.8481

0.1519

7.60

895.53

16

4.0x10 "3

3.5034x10 "3

0.4966 x10 "3

2.48

708.7

17

2.0

1.5485

0.4515

2.26

1457.9

18

1.8

1.3663

0.4337

2.17

1587.1

19

1.6

1.2022

0.3978

1.99

1654.5

20

1.4

1.0567

0.3433

1.72

1624.4

21

8.0 x 10 "4

6.3923 x IO "4

1.6077 x10 "4

0.80

1258

22

6.0

4.4970

1.5030

0.75

1671

23

4.0

2.7814

1.2186

0.61

2191

24

2.0

1.4043

0.5957

0.30

2121

25

1.6

1.2889

0.3111

0.16

1207

26

1.0

0.8244

0.1756

0.09

1065

7

620,098

Table V. Absorption of benzyl alcohol on Soyamine 90, in the presence of milk

Point

C0 M / L

CfM / L

Cb M / L

cb r

f 2 x IO "4

Q

1

2.0 x 10 "1

1.8850 x 10 "1

0.1150 xlO "1

57.50

405.04

2

1.8

1.6876

0.1224

56.20

333.02

3

1.6

1,5007

0.0993

49.65

330.85

4

1.4

1.3279

0.0721

36.05

271.48

5

1.2

1.1182

0.0818

40.90

365.77

6

1.0

0.9313

0.0687

34.35

368.84

7

6.0x10 "2

5.6638x10 "2

0.3362 xlO "2

16.81

296.80

8

4.0

3.8529

0.1471

7.36

190.90

9

2.0

1.9264

0.0736

3.68

191.03

10

1.8

1.7505

0.0495

2.48

141.39

11

1.6

1.5475

0.0525

2.63

169.63

12

1.4

1.3594

0.0406

2.03

149.33

13

1.2

1.1740

0.0260

1.30

110.73

14

1.0

0.9679

0.0321

1.605

165.82

15

6.0x10 "3

5.9039 xlO "3

0.0961 x 10 "3

0.481

81.40

16

4.0

3.9011

0.0989

0.495

126.8

17

2.0

1.9169

0.0831

0.416

216.8

18

1.8

1.7270

0.0730

0.365

211.3

19

1.6

1.5532

0.0468

0.234

150.7

20

1.4

1.3464

0.0536

0.268

199.0

21

1.2

1.1873

0.0127

0.064

53.5

22

1.0

0.9780

0.0220

0.110

112.5

23

8.0 x 10 "4

7.8576 xlO "4

0.1424 x 10 "4

0.071

91

24

6.0

5.8250

0.1750

0.088

150

25

4.0

3.8858

0.1142

0.057

147

26

2.0

1.9552

0.0448

0.022

115

27

1.6

1.5537

0.0463

0.023

149

28

1.0

0.9765

0.0235

0.012

120

12 sheets of drawings