Bitterness in Bacillus proteinase hydrolysates of whey proteins

Spellman, David; O'cuinn, Gerard; Fitzgerald, Richard J.

doi:10.1016/j.foodchem.2008.09.067

Cited by 109 publications

(88 citation statements)

References 32 publications

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“…Hydrolysis has the potential to release specific peptide sequences with bioactive potential, previously encrypted within the protein 110 structure. 48 As expected, enrichment in bioactive peptides correlated with the enrichment of smaller molecular mass peptides following the two UF steps. Bioactivity was found in the 5 and 1 kDa retentates possibly due to the fact that they still contained bioactive peptides as the UF procedure employed did not include a diafiltration step.…”

supporting

confidence: 69%

“…Detection of peptides and proteins was carried out at 214 nm. Separation of the peptides was carried out as described in Spellman et al 48 Milk proteins (NaCN, Acid CN, SMP and GMP), hydrolysates (NaCNH, Acid CNH-240 min, SMPH-240 min and GMPH-240 10 min), SPE fractions and isoelectric focusing (IEF) fractions of NaCNH-240 min were analysed by liquid chromatography using a UPLC (Acquity, Waters, Dublin, Ireland) as described by Nongonierma and FitzGerald 49 . Separation of peptides and individual milk proteins was carried out at 30C, using a 2.1 x 15 100 mm, 1.7 µm Acquity UPLC C18 BEH column mounted with a 0.2 µm inline filter (Waters, Dublin, Ireland).…”

Section: Hydrolysis Of Milk Protein Substratesmentioning

confidence: 99%

“…The molecular mass distribution profiles of the proteins and peptides present in the NaCN, NaCNH and associated UF 20 fractions of NaCNH-240 min sample were determined by gel permeation chromatography -high performance liquid chromatography (GPC-HPLC) essentially as described by Spellman et al 48 The freeze-dried samples were resuspended in the mobile phase …”

Section: Simulated Intestinal Digestionmentioning

confidence: 99%

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Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the starting substrate and isolation of bioactive fractions

et al. 2013

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Milk protein hydrolysates generated with different starting substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT 2c ) receptor agonists. The 5-HT 2c receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to 10 enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only starting substrate showing 5-HT 2c serotonin receptor agonist activity. The 5-HT 2c serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semipreparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing 15 (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (< 1 kDa), were hydrophobic in nature and had a pI between 8.6 and 13.2. These different physicochemical characteristics together with the stability of NaCNH-240 min to simulated intestinal digestion, allow prediction of a favourable outcome regarding the bioavailability of the bioactive peptides therein. These results reinforce the potential of milk-derived bioactive peptides to 20 be developed into functional foods targeted at 5-HT 2c receptor modulation.

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supporting

confidence: 69%

Section: Hydrolysis Of Milk Protein Substratesmentioning

confidence: 99%

Section: Simulated Intestinal Digestionmentioning

confidence: 99%

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Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the starting substrate and isolation of bioactive fractions

et al. 2013

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“…In this regard, Aubes-Dufau et al (1995) mentioned that the peptides with molecular weights up to roughly 6 kDa and Q values exceeding 1400 cal¢mol ¡1 can be considered bitter; Q value is a predictive index for bitterness of a given peptide and is defined as the hydrophobicity of the side chain of amino acids in the peptide (Ney, 1971). Bitterness of hydrolysates is not only caused by hydrophobic amino acid themselves but by their locations in peptide sequence, as well (Spellman et al, 2009). Hydrophobic amino acids caused more bitterness when they were inside the peptide chain rather than the N-or C-terminus of peptides (Matoba and Hata, 1972).…”

Section: Removing Bitternessmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

138

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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“…It is also known that the hydrolysis of protein produces peptides with brownish color and that the addition of large quantities of protein hydrolysate can affect the color of the product (Bueno-Solano et al, 2009). Moreover, other studies reported that the major disadvantage of the use of protein hydrolysates is the occurrence of bitter peptides (Spellman et al, 2009). It is likely that the bitter taste of these peptides can be experienced in the products and, therefore, this is the reason why T2 and T3 obtained lower scores (P < 0.05) for the taste parameter.…”

Section: Sensory Evaluationmentioning

confidence: 99%