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1

The pancreatic proteolytic enzymes of African ostrich

100%
Zelazko M., Chrzanowska J., Polanowski A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
2

Oszacowanie pobrania barwników syntetycznych przez wybraną grupę dzieci

100%
Sicinska E., Zelazko M., Brzozowska A.
Bromatologia i Chemia Toksykologiczna
|
2010
|
tom 43
|
nr 4
3
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Application of pancreatic enzymes in hydrolysis of egg-white proteins

100%
Graszkiewicz A., Zelazko M., Trziszka T.
Polish Journal of Food and Nutrition Sciences
|
2010
|
tom 60
|
nr 1
The hydrolysis of egg-white protein precipitate (EWPP) with trypsin, chymotrypsin, and elastase was studied. The peptides obtained were determined for their antioxidative properties. Chymotrypsin caused the most extensive degradation of EWPP. The degrees of hydrolysis (DHs) of the one‑hour hydrolysates were 77.6%, 55.8%, and 43.3% for chymotrypsin, trypsin, and elastase, respectively. Only small peptides with molecular weights of 5-10 kDa (74.2%) and <3 kDa (25.6%) were found in the one-hour hydrolysate with chymotrypsin, whereas products with higher molecular weights (78 kDa, 37 kDa, 34 kDa, and 78 kDa, respectively) as well as the small peptides were produced with elastase and trypsin. In the ensuing hours the rate of hydrolysis slowed and the DHs of the final hydrolysates were 95.8%, 95.3%, and 79.9% for trypsin, chymotrypsin, and elastase. The RP-HPLC profiles of the final hydrolysates showed differences in the hydrophobicity of the generated peptides. All hydrolysates exhibited weak scavenging activity of DPPH free radicals.
4

Proteinazy trzustkowe - zroznicowanie miedzygatunkowe i wynikajace z tego implikacje zywieniowe i biotechnologiczne

100%
Zelazko M., Chrzanowska J., Polanowski A.
Biotechnologia
|
2007
|
nr 1
107-120
5
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Antioxidative capacity of hydrolysates of hen egg proteins

100%
Graszkiewicz A., Zelazko M., Trziszka T., Polanowski A.
Polish Journal of Food and Nutrition Sciences
|
2007
|
tom 57
|
nr 4[A]
195-199
The antioxidant capacity as free radicals of 1,1 diphenyl-2-picryhydrazyl (DPPH) scavenger of egg white protein hydrolysate was investigated. Egg white protein precipitate obtained as a by-product in cystatin and lysozyme isolation was hydrolysed with bovine trypsin and then separated by means of RP-HPLC. Of ten fractions collected only no. 2 (0.195 μmol Trolox /mg) and no. 5 (0.186 μmol Trolox /mg) displayed a considerable free radicalscavenging capacity. The rechromatography of these fractions yielded four products of raised antioxidant activity: no. 2E (obtained from fraction no. 2) and no. 5E, 5F, 5H (obtained from fraction no. 5) which amounted to 0.482 μmol Trolox /mg and 0.584, 1.375, 1.200 μmol Trolox /mg, respectively.
6

Białka jaja kurzego: prekursory bioaktywnych peptydów

100%
Zambrowicz A., Zelazko M., Trziszka T.
Medycyna Weterynaryjna
|
2011
|
tom 67
|
nr 03
Biologically active peptides are of particular interest to food science and nutrition because they may act as potential physiological modulators of metabolism. Hidden or inactive in the amino-acid sequence of food proteins, they can be released or activated in vivo during gastrointestinal digestion, or in vitro during enzymatic hydrolysis and food processing. Egg proteins are an important source of these bioactive peptides. In recent years, major egg protein components, ovoalbumin, conalbumin, ovomucin and phosvitin, have also been shown to contain bioactive sequences. Peptides showing antiadhesive, anticancer as well as immunomodulatory activities were found in ovomucin sequence. Immunoregulative peptides were also found in peptic and chymotryptic hydrolysates of ovoalbumin. Ovocinin and ovocinin(2-7) - angiotensin-converting enzyme inhibitory peptides, whose pharmacological activity was observed in micromolar concentrations - were liberated during in vitro proteolysis of ovoalbumin. Furthermore, many egg protein hydrolysates showed antimicrobial and antioxidant activity after proteolysis with different enzymes, and several active peptides were isolated and identified.
7

Wzrost i enzymatyczna aktywność drożdży w mleku różnych gatunków przeżuwaczy

88%
Szoltysik M., Zelazko M., Polomska X., Wojtatowicz M., Chrzanowska J.
Acta Scientiarum Polonorum. Biotechnologia
|
2008
|
tom 07
|
nr 2
8

Use of yeast enzymes in degradation of paracasein curd

88%
Niedbalska J., Szoltysik M., Zelazko M., Dabrowska A., Chrzanowska J.
Polish Journal of Food and Nutrition Sciences
|
2007
|
tom 57
|
nr 4[B]
9

Produkcja pozakomórkowych hydrolaz przez szczepy Yarrowia lipolytica pochodzące z sera

76%
Szoltysik M., Chrzanowska J., Zelazko M., Niedbalska J., Polomska X., Juszczyk P., Wojtatowicz M.
Acta Scientiarum Polonorum. Biotechnologia
|
2008
|
tom 07
|
nr 4
10

Zdolnosc drozdzy Yarrowia lipolytica pochodzacych z sera do wytwarzania amin biogennych w mleku

76%
Szoltysik M., Zelazko M., Rak L., Polomska X., Dabrowska A., Wojtatowicz M., Chrzanowska J.
Acta Scientiarum Polonorum. Biotechnologia
|
2006
|
tom 05
|
nr 1-2
87-94
11

Non-conventional affinity chromatography of serine proteinases and their inhibitors

76%
Polanowski A., Wilimowska-Pelc A., Kowalska J., Grybel J., Zelazko M., Wilusz T.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 3
From among a wide variety of protein purification techniques affinity chromatogra­phy has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na+ but not K+ or Li+ ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and arproteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inac­tive derivative methylchymotrypsin in the presence of 5 M NaCl.
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