2014
DOI: 10.1016/j.procbio.2014.08.009
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Influence of water availability on the enzymatic hydrolysis of proteins

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Cited by 27 publications
(17 citation statements)
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“…In particular, in the hydromodule 1:2, the higher substrate concentration lead to a higher release of N-species during the first hour, compared to the other ratio, but with a lower value at the end of the reaction, (%DH=17.3 ± 0.1). Conversely, the more diluted solution with hydromodule 1:3, generated more N-free species at the end of the hydrolysis reaction (%DH = 19.2 ± 0.2), consistent with the findings of Butrè et al (2014a). The latter authors demonstrated that water availability plays a crucial role in the hydrolysis of proteins (at constant enzyme/substrate ratio) by increasing protein concentration and decreasing the overall rate of enzymatic protein hydrolysis.…”
Section: Enzymatic Hydrolysis At Lab-and Medium-scalesupporting
confidence: 85%
“…In particular, in the hydromodule 1:2, the higher substrate concentration lead to a higher release of N-species during the first hour, compared to the other ratio, but with a lower value at the end of the reaction, (%DH=17.3 ± 0.1). Conversely, the more diluted solution with hydromodule 1:3, generated more N-free species at the end of the hydrolysis reaction (%DH = 19.2 ± 0.2), consistent with the findings of Butrè et al (2014a). The latter authors demonstrated that water availability plays a crucial role in the hydrolysis of proteins (at constant enzyme/substrate ratio) by increasing protein concentration and decreasing the overall rate of enzymatic protein hydrolysis.…”
Section: Enzymatic Hydrolysis At Lab-and Medium-scalesupporting
confidence: 85%
“…The main peak (78%) was identified to be the enzyme BLP (23.6 kDa). A second smaller peak (14% of total UV 214 area) was due to the pro-peptide (6.9 kDa) as described previously [17]. The enzyme has an activity of 3.9 AU/mg/min as determined by the azocasein assay.…”
Section: Methodsmentioning
confidence: 64%
“…The BLP (4.5% (w/w) protein, by the Dumas method N × 6.25; activity of 0.3 AU/mg/min as determined by the azocasein assay [16]) was partly insoluble and was fractionated as described before [17]. The freeze dried, water soluble material was found to contain 60% (w/w) protein (N × 6.25).…”
Section: Methodsmentioning
confidence: 99%
“…While the proteases used in this study have specificity for the breakdown of proteins, Alcalase has a preference for large residue carboxyl sites without load of proteins and peptides links to adjacent hydrophobic or aromatic amino acids, such as tyrosine (Butré, Wierenga, & Gruppen, ; Paraman, Hettiarachchy, Schaefer, & Beck, ; Rossini, Noreña, Cladera‐Olivera, & Brandelli, ). Even though the specificities of Neutrase and Protamex are not clearly defined (Dryáková, Pihlanto, Marnila, Čurda, & Korhonen, ), it is known that they are endoproteases characterized by their ability to hydrolyze internal peptides bonds (Liu et al, ), which preferentially release hydrophobic amino acids: phenylalanine, isoleucine, leucine, methionine, and valine (Dijk, Folkertsma, & Dekker, ).…”
Section: Resultsmentioning
confidence: 99%
“…While the proteases used in this study have specificity for the breakdown of proteins, Alcalase has a preference for large residue carboxyl sites without load of proteins and peptides links to adjacent hydrophobic or aromatic amino acids, such as tyrosine (Butré, Wierenga, & Gruppen, 2014;Paraman, Hettiarachchy, Schaefer, & Beck, 2007;Rossini, Noreña, Cladera-Olivera, & Brandelli, 2009).…”
Section: Nutritional and Bioactive Resultsmentioning
confidence: 99%