Separation of low molecular weight rapeseed proteins by RP-HPLC-DAD - a short report

Kosinska, A.; ChavanUD,; Amarowicz, Ryszard

doi:10.17221/3292-cjfs

Cited by 4 publications

(1 citation statement)

References 4 publications

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“…The GE in samples of food, feces, and urine was determined using an isoperibol bomb calorimeter (model C2000 basic, Ika-Werke, Staufen, Germany). The protein molecular weight analysis of both types of feather meal was performed by HPLC with an ultraviolet detector according to the methodology used by Kosińska et al (2006). All analyses were performed in duplicate assuming the standard error between replicates of less than 5% for all methods and less than 1% for energy.…”

Section: Methodsmentioning

confidence: 99%

Inclusion of exogenous enzymes to feathers during processing on the digestible energy content of feather meal for adult dogs

et al. 2016

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-This study was conducted to determine the coefficient of total tract apparent digestibility (CTTAD) of nutrients and gross energy (GE), metabolizable energy (ME), coefficient of metabolizability of gross energy (CM of GE), and fecal characteristics of dogs fed diets with two levels of feather meal, with or without addition of an enzyme blend containing lipase and protease activity. Ten adult Beagle dogs (aged between 1 and 2 years and weighing 10.2±1.4 kg) were arranged in a 5 × 3 incomplete Latin square design with five treatments and three periods. The extruded basal diet was provided in equal amounts to all dogs (220 g/d), and 7.5 and 15% of hydrolyzed feather meal without enzymes (HFM) or HFM processed with addition of the enzyme blend (HFM EB) was added on top of the basal diet just before feeding. The contrast analysis showed that inclusion of 7.5 or 15% feather meal negatively affected CTTAD of crude protein (CP), GE, and ME of the diets with no apparent effect of the enzyme treatment. However, when both feather meal samples were evaluated, the HFM EB resulted in better CTTAD of GE and CM of GE (0.774 vs. 0.666) than HFM without enzymes (0.670 vs. 0.567), respectively. There was no effect of either feather meal on fecal score. Regression analysis showed that the enzymes added to the feathers during the digestion process increased digestible energy by 600 kcal/kg of dry matter in the diet containing HFM EB. High-performance liquid chromatography (HPLC) analysis demonstrated that feather meal had a low molecular weight, with about 95% of the molecules below 10,000 Da. Addition of enzymes during the feather hydrolysis process may improve the energy content of the feather meal when included in diets for adult dogs.

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Section: Methodsmentioning

confidence: 99%

Inclusion of exogenous enzymes to feathers during processing on the digestible energy content of feather meal for adult dogs

et al. 2016

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SE-HPLC separation of myosin complex with tannins from bearberries (Arctostaphylos uva-ursi L. Sprengel) leaves - a short report.

Amarowicz¹,

Pegg²,

Kosińska³

2009

Czech J. Food Sci.

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Amarowicz R., Pegg R.B., Kosińska A. (2009): SE-HPLC separation of myosin complex with tannins from bearberries (Arctostaphylos uva-ursi L. Sprengel) leaves -a short communication. Czech J. Food Sci., 27: 386-391.Phenolic compounds were extracted from bearberry (Arctostaphylos uva-ursi L. Sprengel) leaves into 95% (v/v) ethanol. The tannin constituents were separated from the crude extract using Sephadex LH-20 column chromatography with 95% (v/v) ethanol and 50% (v/v) acetone as the mobile phases. Myosin was isolated and purified from excised pork knuckle muscles using the standard salt-solution extraction procedure followed by gel filtration chromatography. Myosin was precipitated from the solution with bearberry-leaf tannins at pH 5.0. The recovered complex was washed, lyophilised, and subjected to size-exclusion high performance liquid chromatography (SE-HPLC). Based on the basic conditions of the HPLC analysis, a portion of the tannin constituents was liberated from the complex. The UV spectra of these compounds were characterized by a maximum at ~ 300 nm. A portion of the tannins was present in the complex with myosin, and this was confirmed by UV spectra.

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Presence of ferulic acid in wheat glutenin fraction and its enzymatic hydrolysates - a short report

Karamać¹,

Sendrejova²,

Kosińska³

et al. 2007

Czech J. Food Sci.

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Three protein fractions: albumin-globulin, gliadin, and glutenin were extracted from wheat grains. Enzymatic hydrolysates were obtained from each fraction using trypsin, protease from <I>Bacillus subtilis</I> and Subtilisin Carlsberg. Ferulic acid was detected neither in albumin-globulin and gliadin fractions nor in their hydrolysates. The RP-HPLC and SE-HPLC chromatograms of the glutenin fraction and its hydrolysates revealed the presence of peaks originated from ferulic acid and ferulic acid derivative/complex. The content of ferulic acid in the glutenin fraction was 1.12 mg/g. During HPLC analysis, the peptide products of glutenin hydrolysis should be recorded at 220 nm because the peaks of the peptides recorded at 280 nm can be overlapped by the peaks of ferulic acid and its derivatives.

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Separation of low molecular weight rapeseed proteins by RP-HPLC-DAD - a short report

Cited by 4 publications

References 4 publications

Inclusion of exogenous enzymes to feathers during processing on the digestible energy content of feather meal for adult dogs

Inclusion of exogenous enzymes to feathers during processing on the digestible energy content of feather meal for adult dogs

SE-HPLC separation of myosin complex with tannins from bearberries (Arctostaphylos uva-ursi L. Sprengel) leaves - a short report.

Presence of ferulic acid in wheat glutenin fraction and its enzymatic hydrolysates - a short report

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