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......................................................................................................................................... 8
1. ............................................................10
1.1. ..........................................................12
1.1.1. ............................................................................................................... 12
1.1.2. (......................................................................................13
1.1.3. .............................................................................................. 14
1.1.4. ........................................................................................16
1.2. .................................... 18
1.2.1. ....................................................................................................... 18
1.2.2. ................................................................................................. 19
1.2.3. ...............................................................................................20
1.2.4. .................................................................................................................. 21
1.3. ................................... 23
1.3.1. .......................................................................................................23
1.3.2. ............................................................................................24
1.4. ...........................................................................................................................24
1.5. ..........................................................................................25
1.6. ............................................................................................ 25
1.7. ........................................................................................25
1.8. .............................................................................................................26
2. 27
...........................................................................................................................30

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PAGINACIJA STRANA NIJE DOBRA!!! KORIGOVATI TO NA LAPTOPU U DOCX


FORMATU!




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ANTINUTRITIVE SUBSTANCES OF PLANT ORIGIN IN ANIMAL FEED


Summary
Antinutritive substances are substances of plant origin that decrease the efficiency of
utilization of nutrients and meal. It is therefore very important to know how to identify them,
and procedures for their inactivated to preserve the maximum nutritional value.
The group of these substances include: enzyme inhibitors, antivitamins, substances
that bind minerals and other toxic substances that are naturally found in feeds.
So far identified a number of such substances, which do not show lethal effect, or it
occurs only in cases when animals ingested over a certain amount. The nutrition of domestic
animals and especially those with high genetic potential, today it is very interesting nutrients
that are rich in biologically high-value proteins with a solid or a good concentration of energy.
This group primarily includes annual grain legumes (soybean, legumes, peas, lentils, etc.) and
the corresponding products based on them. The biological value of these nutrients is such that
allows partial, and in certain types and categories and complete substitution of expensive
animal protein sources in the diet, as these nutrients seem to date and from an economic point
of view. However, most of the nutrients contained in fruits and their products based on them
larger or smaller amounts of antinutritive substances which certainly reduces the effectiveness
of their use.
In the last two to three decades of state procedures for removing and inactivating them
and the possibility of producing different varieties of plants with greatly reduced quantities of
these substances (without the Kunitz soybean trypsin inhibitor). Appropriate heat treatment is
most undesirable substances partially or completely inactivated. However it is known that
each temperature treatment causes denaturation of protein nutrients and reduce their solubility
in water. Due to decreased protein solubility and digestibility decreases.
Different materials are antinutritive, with different amounts, represented in the plant
world, but, of course, there is plenty of legumes and some grains.
Keywords: antinutritive matter, legumes, adverse effects



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Ta 1. 100 . (o, o) (USDA Nutrient


Database)

30.16 g

36.49 g
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7.33 g

- T

0.591 g

9.3 g

- T

1.766 g

19.94 g

1.971 g

2.884 g

3.309 g

4.404 g

2.706 g

11.255 g

0.547 g

8.54 g

0.655 g

A.

1 g

2.122 g

0.377 mg

1.539 g

12

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2.029 g

115.9 mg

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3.153 g

6.0 mg

1.097 g

47 g

- A

1.915 g

277 mg

- A

5.112 g

15.70 mg

7.874 g

704 mg

1.880 g

1797 mg

2.379 g

2 mg

2.357 g

4.89 mg

280 mg

1 g

Vitamin 6

0.377 mg

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A
1. , , , , 2005, Biologically active

components of soybeans and soy protein products. Acta Periodica Technologica, 36,1266,
2. , , , , , , 2010,

, XXIV
, , . 16, . 3-4, 143-154,
3. Bell, J.M. 1974. Nutritional value of low glucosinolate rapeseed meal forswinw. Can.

J. Anim. Sci. 55: 6l-70.,


4. Birk, Y, 1961, Purification and some properties of a highly active inhibitor of tripsin

and -chymotrypsin from soybeans. Biochim. Biophys, Acta. 54, 378-381,


5. Bowman, D.E, 1944, Fractions derived from soy beans and navy beans which retard

triptic digestion of casein. Proc. Soc. Exp. Biol. Med. 57, 139-140,
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Publishing Inc. West Port, Connecticut,


7. Davie, S.R, Dalais, F.S, Simpson, E.R, Murkies, A.L, 1999, Phytoestrogens in health

and disease. Recent Prog. Horm. Res., 54, 185-210,


8. Friedman, M, Brandon, D.L, Bates, A.H, Hymowitz, T, 1991, Comparison of a

commercial soybean cultivar and an isoline lacking the Kunitz trypsin inhibitor:
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Potential of Soybean Lectin and Lunasin. Nutrit. Rev. 61, 239-246.,


10. Harborne, J.B, 1989, Biosynthesis and function of antinutritional factors in plants,

Aspects of Applied Biology 19, 21-28,


11. Hymowitz, T, 1986, Genetics and breeding of soybeans lacking the Kunitz trypsin

inhibitor. Pages 291-298 in Nutritional aqnd Toxicological Significance of Enzyme


Inhibitors in Foods. M.Friedman, ed. Plenum Press, New York, NY,
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Isolated from Soybean.J. Agric. Food Chem 51, 7901-7906,


13. Kumar R, 1992, Antinutritional factors, The potential risks of toxicity and the methods

to alleviate them, In: Legume trees and other fodder trees as protein source for

31

livestock. FAO Animal Production and Health Paper No. 102. (Edited By A W Speedy
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668-669,
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,
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antinutritive factors and fibrous feedstuffs in pig diets on amino acid digestibilities
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