Towards predicting protein hydrolysis by bovine trypsin

Deng, Yongkai; Veer, Frank van der; Sforza, Stefano; Gruppen, Harry; Wierenga, Peter A.

doi:10.1016/j.procbio.2017.11.006

Cited by 44 publications

(96 citation statements)

References 36 publications

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“…There are a considerable number of studies regarding the hydrolysis of foods and its relation with the generation of bioactive peptides. For instance milk, meat, fish, eggshell membrane proteins and plant by-products were hydrolysed using trypsin (Deng, Veer, Sforza, Gruppen and Wierenga, 2017), pepsin (Xu, Cao, He and Yang, 2009), chymotrypsin (Wei and Chiang, 2009), papain (Xu et al, 2009), Alcalase (Shi, Kovacs-Nolan, Jiang, Tsao and Mine, 2014), or Corolase PP (Coscueta, Amorim, Voss, Nerli, Picó and Pintado, 2016;Guan, Diao, Jiang, Han and Kong, 2018). Wiriyaphan, Chitsomboon and Yongsawadigu (2012), Moayedi, Mora, Aristoy, Hashemi, Safari and Toldrá (2016) and Lassoued, Mora, Barkia, Aristoy, Nasri and Toldrá (2016) reported that the hydrolysis of food proteins by pepsin, trypsin, Alcalase and Bacillus subtilis A26 proteases leads to the generation of antioxidant and ACE-inhibitory peptides.…”

Section: Introductionmentioning

confidence: 99%

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Maqsoudlou

Mahoonak

Mora

et al. 2019

Food Research International

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Peptides with a similar antioxidant and ACE-inhibitory activity of royal jelly (RJ) generated from Alcalase hydrolysated pollen (AHP) were predicted by Response Surface Methodology (RSM). Later, AHP was prepared and deproteinised to be further analysed using size-exclusion chromatography (SEC). After SEC separation, fractions 49-57, 64-66 and 52-54 of AHP and fractions 43-55 of RJ that showed the highest ACE-inhibitory, DPPH radical scavenging and ferric-reducing power activities, were purified by RP-HPLC. After the separation of fractions 49-57 of AHP, fractions eluting at 3, 4, 5, 37 and 60 min and fractions eluting at 12 to 33 min showed ACE-inhibitory activity higher than 80% whereas fraction eluting at 34 min showed the highest DPPH scavenging activity. 195 peptide sequences were identified by nano-liquid chromatography and mass spectrometry in tandem (nLC-MS/MS). The origins of all identified peptides were herbal proteins and certain similarities with previously described bioactive sequences were discussed.

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Section: Introductionmentioning

confidence: 99%

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Maqsoudlou

Mahoonak

Mora

et al. 2019

Food Research International

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“…The mass tolerance for the accepted annotation was ≤10 ppm between the theoretical mass and the measured mass, which is generally accepted for this type of equipment and method . Furthermore, each of the peptide identifications are confirmed by the presence of at least one of their b/y fragments.…”

Section: Methodsmentioning

confidence: 99%

Identification of a TLR2 Inhibiting Wheat Hydrolysate

Kiewiet

Dekkers

Gool

et al. 2018

Molecular Nutrition Food Res

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Scope Wheat hydrolysates are used in medical nutrition to provide undernourished patients a readily digestible protein source, for instance to recover from chemotherapy‐induced intestinal mucosal inflammation. Since many hydrolysates of different sources can modulate the immune system, likely via Toll‐like receptors (TLRs), it is hypothesized that also wheat hydrolysates might interact with TLR signaling, which could be a way to prevent intestinal inflammation and damage. Methods and results The capacity of three wheat hydrolysates to modulate immunity by interfering with TLR signaling is determined. All wheat hydrolysates have TLR modulating effects but only one has strong TLR2 inhibiting effects, attenuating both TLR2/1 and TLR2/6 signaling in a reporter cell system. This is likely induced by direct TLR2‐ectodomain binding, as confirmed by ELISA. Furthermore, this TLR2 blocking hydrolysate reduces IL‐6 production in human dendritic cells. Application of reversed‐phase–ultra HPLC combined with MS reveals that the presence of peptide WQIPEQSR is associated with the observed TLR2 inhibiting capacity. Conclusion The study demonstrates TLR2‐inhibiting capacities of a wheat hydrolysate. The findings provide a good start for further research to investigate whether this hydrolysate might contribute to the management of intestinal mucosal inflammation in cancer patients receiving chemotherapy.

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“… 1 Peptide analysis showed that the lower DH max,exp reached by bovine trypsin was due to 8 of the 14 cleavage sites (CSs) on the protein being hydrolyzed by the enzyme only at low rates. 2 It was proposed that these low hydrolysis rate constants were due to the hindrance of bovine trypsin by the charged AAs surrounding the CSs ( Table 1 ). 2 The differences in the hydrolysis rate constants of CSs in a protein are quantitatively described by enzyme selectivity.…”

Section: Introductionmentioning

confidence: 99%

“… 2 It was proposed that these low hydrolysis rate constants were due to the hindrance of bovine trypsin by the charged AAs surrounding the CSs ( Table 1 ). 2 The differences in the hydrolysis rate constants of CSs in a protein are quantitatively described by enzyme selectivity. 3 The current study aims to investigate hydrolysis by bovine, porcine, and human trypsins and to determine if the differences in DH max,exp could be explained based on the enzyme selectivity.…”

Section: Introductionmentioning

confidence: 99%

“… 4 Unless stated otherwise, in this study, bovine and porcine trypsins refer to trypsin-1, and human trypsin refers to trypsin-2. For bovine trypsin, the experimental maximum degrees of hydrolysis (DH max,exp ) of α-lactalbumin, β-casein, and β-lactoglobulin were reported to be 5.1, 2 4.3, 2 and 8.0%, 2 , 5 respectively. These values were only 48, 60, and 75% of the theoretical maximum degrees of hydrolysis (DH max,theo ) of the proteins.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins

Deng

Gruppen

Wierenga

2018

J. Agric. Food Chem.

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Based on trypsin specificity (for lysines and arginines), trypsins from different sources are expected to hydrolyze a given protein to the same theoretical maximum degree of hydrolysis (DHmax,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DHmax (DHmax,exp) by bovine, porcine, and human trypsins are due to their secondary specificity. Peptide analysis showed that ∼78% of all the cleavage sites were efficiently hydrolyzed by porcine trypsin, and ∼47 and ∼53% were efficiently hydrolyzed by bovine and human trypsins, respectively. These differences were explained by the enzyme secondary specificity, that is, their sensitivities to the amino acids around the cleavage sites. The DHmax predictions based on the secondary specificity were 4 times closer to the DHmax,exp than the predictions based on trypsin specificity alone (DHmax,theo). Proposed preliminary relations between binding sites and trypsin secondary specificity allow DHmax,exp estimations of tryptic hydrolysis of other proteins.

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Towards predicting protein hydrolysis by bovine trypsin

Cited by 44 publications

References 36 publications

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Identification of a TLR2 Inhibiting Wheat Hydrolysate

Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins

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