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Application of aluminosilicates for mitigation of ammonia and volatile organic compound emissions from poultry manure

100%

Opaliński S., Korczyński M., Szołtysik M., Dobrzański Z., Kołacz R.

Open Chemistry

2015

vol. 13

issue 1

Odor mitigation techniques are widely investigated due to the problem of odor nuisance generated by intensive livestock production. The goal of this research was to investigate the use of aluminosilicate sorbents as filter packs in the air scrubber ODOR1, which enables cleaning of air inside the livestock building. The following sorbents were examined: raw halloysite, roasted halloysite, activated halloysite, raw bentonite, roasted bentonite and expanded vermiculite. The experiment was conducted in chambers where poultry manure was placed, the time of air treatment was 24 hours. A manual SPME (solid-phase microextraction) holder with DVB/Carboxen/PDMS fiber was used for extraction of odor compounds, and analyses were carried out using gas chromatography-mass spectrometry. Ammonia concentrations were determined according to Polish standards (Nessler method) using a spectrophotometer. It was found that all examined aluminosilicates had the potential for removal of ammonia as well as 24 volatile compounds emitted from poultry manure. The highest efficiency was noted for activated halloysite (81%) and roasted bentonite (84%) in the case of ammonia and odors, respectively. Despite the limitations of the study, the results showed the effectiveness of the air scrubber packed with aluminosilicates for the reduction of volatile odorous compounds in the air of livestock buildings.

Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein

86%

Dąbrowska A., Szołtysik M., Babij K., Pokora M., Zambrowicz A., Chrzanowska J.

2013

vol. 60

issue 1

117-122

The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC peptide profiles and by polyacrylamide gel electrophoresis. In all hydrolyzates analyzed antioxidant activities were determined using three tests: the ability to reduce iron ions in FRAP test, the ability to scavenge free radicals in DPPH test, and Fe2+ chelating activity. The antimicrobial activity of obtained peptide fractions was determined as the ability to inhibit the growth of Escherichia coli, Bacillus cereus and Pseudomonas fluorescens in a diffusion plate test. The deepest degradation, expressed as the DH [%] and the free amino group content (67% and 7528 µmole Gly/mg, respectively), was noted in samples hydrolyzed with 300 U/ml of enzyme for 24 hours, while in other samples the determined values were about three and two times lower. The results were in agreement with the peptide profiles obtained by RP HPLC. The highest antioxidative activities determined in all tests were seen for the casein hydrolysate obtained with 300 U/mg protein of serine proteinase after 24 h of reaction (2.15 µM Trolox/mg, 96.15 µg Fe3+/mg, 814.97 µg Fe2+/mg). Antimicrobial activity was presented in three preparations. In other samples no antimicrobial activity was detected.

The use of serine protease from Yarrowia lipolytica yeast in the production of biopeptides from denatured egg white proteins

73%

Pokora M., Zambrowicz A., Zabłocka A., Dąbrowska A., Szołtysik M., Babij K., Eckert E., Trziszka T., Chrzanowska J.

2017

vol. 64

issue 2

245-253

Deriving non-conventional enzymes from cheaper sources than those used for commercially available enzymes may result in the production of hydrolysates with beneficial features, while drastically reducing the cost of hydrolysis. This is especially significant for enzymatic hydrolysis as a method of protein waste utilization. We have previously described the ability of non-commercial serine protease from Yarrowia lipolytica yeast to produce/release bioactive peptides from egg white protein by-products (EP). The enzymatic hydrolysis of EP was carried out for 24 h using the serine protease at an enzyme: substrate ratio of 1:30 (w/w). The obtained hydrolysate was characterized by protein degradation of 38% and also exhibited an antioxidant and cytokine-inducing activity. The isolation procedure (ultrafiltration and RP-HPLC) of bioactive peptides from the EP hydrolysate provided peptide fractions with significant antioxidant and ACE inhibitory activities. Three homogeneous and three heterogeneous peptide fractions were identified using MALDI-TOF/MS and the Mascot Search Results database. The peptides, mainly derived from ovalbumin, were composed of 2-19 amino-acid residues. We have thus demonstrated a novel ability of serine protease from Y. lipolytica to release biopeptides from an EP by-product.

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2 Acta Biochimica Polonica

1 Open Chemistry

1 2017

1 2015

1 2013

3 Szołtysik M.

2 Babij K.

2 Chrzanowska J.

2 Dąbrowska A.

2 Pokora M.

2 Zambrowicz A.

1 Dobrzański Z.

1 Eckert E.

1 Korczyński M.

1 Kołacz R.

1 Opaliński S.

1 Trziszka T.

1 Zabłocka A.

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Application of aluminosilicates for mitigation of ammonia and volatile organic compound emissions from poultry manure

Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein

The use of serine protease from Yarrowia lipolytica yeast in the production of biopeptides from denatured egg white proteins