Protein Hydrolysates

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 7350 Experts worldwide ranked by ideXlab platform

Rotimi E. Aluko - One of the best experts on this subject based on the ideXlab platform.

  • Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors
    2019
    Co-Authors: Temitola O. Awosika, Rotimi E. Aluko
    Abstract:

    In this work, we report the potency of enzymatic Hydrolysates of pea Proteins against trypsin and chymotrypsin. Pea Protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the Protein Hydrolysates into peptide fractions ( 3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage.

  • enzymatic Protein Hydrolysates from high pressure pretreated isolated pea Proteins have better antioxidant properties than similar Hydrolysates produced from heat pretreatment
    2015
    Co-Authors: Abraham T Girgih, Dongfang Chao, Lin Lin, Stephanie Jung, Rotimi E. Aluko
    Abstract:

    Isolated pea Protein (IPP) dispersions (1%, w/v) were pretreated with high pressure (HP) of 200, 400, or 600 MPa for 5 min at 24 °C or high temperature (HT) for 30 min at 100 °C prior to hydrolysis with 1% (w/w) Alcalase. HP pretreatment of IPP at 400 and 600 MPa levels led to significantly (P 40%) oxygen radical absorption capacity (ORAC) of Hydrolysates. 2,2-Diphenyl-1-picrylhydrazyl, superoxide radical and hydroxyl radical scavenging activities of pea Protein Hydrolysates were also significantly (P<0.05) improved (25%, 20%, and 40%, respectively) by HP pretreatment of IPP. Protein Hydrolysates from HT IPP showed no ORAC, superoxide or hydroxyl scavenging activity but had significantly (P<0.05) improved (80%) ferric reducing antioxidant power. The Protein Hydrolysates had weaker antioxidant properties than glutathione but overall, the HP pretreatment was superior to HT pretreatment in facilitating enzymatic release of antioxidant peptides from IPP.

  • structural and antihypertensive properties of enzymatic hemp seed Protein Hydrolysates
    2015
    Co-Authors: Sunday A Malomo, Abraham T Girgih, John O Onuh, Rotimi E. Aluko
    Abstract:

    The aim of this work was to produce antihypertensive Protein Hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed Proteins (HSP). The hemp seed Protein Hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed Protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

  • structural and antihypertensive properties of enzymatic hemp seed Protein Hydrolysates
    2015
    Co-Authors: Sunday A Malomo, Abraham T Girgih, John O Onuh, Rotimi E. Aluko
    Abstract:

    The aim of this work was to produce antihypertensive Protein Hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed Proteins (HSP). The hemp seed Protein Hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed Protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

  • blood pressure lowering effects of australian canola Protein Hydrolysates in spontaneously hypertensive rats
    2014
    Co-Authors: Abraham T Girgih, Sunday A Malomo, Adeola M Alashi, Christopher Blanchard, Rodney J Mailer, Samson Agboola, A J Mawson, Rotimi E. Aluko
    Abstract:

    Abstract The in vitro and in vivo antihypertensive activities of canola Protein Hydrolysates and ultrafiltration membrane fractions (

Meram Chalamaiah - One of the best experts on this subject based on the ideXlab platform.

  • Immunomodulatory and anticancer Protein Hydrolysates (peptides) from food Proteins: A review
    2018
    Co-Authors: Meram Chalamaiah, Wenlin Yu, Jianping Wu
    Abstract:

    Bioactive peptides are oligopeptides that consist of 2–20 amino acids that can exert beneficial effects on human health in addition to basic nutritional effects. Food derived Protein Hydrolysates or peptides with immunomodulatory and anticancer activities have been reported from a variety of food Protein sources such as milk, egg, fish, rice, soybean, pea, chlorella, spirulina, oyster and mussel. In vitro hydrolysis of food Proteins using commercial proteolytic enzymes is the most commonly employed process for the production of immunomodulatory and anticancer food Protein Hydrolysates. The immunomodulatory and anticancer activities of food derived Protein Hydrolysates or peptides are related to the amino acid composition, sequence and length. Most immunomodulatory and anticancer food Protein Hydrolysates or peptides were tested using cell culture and animal models, while a few involved clinical trials. This review provides a comprehensive overview of immunomodulatory and anticancer food derived Protein Hydrolysates or peptides, their production and mechanisms of action.

  • antiproliferative ace inhibitory and functional properties of Protein Hydrolysates from rohu labeo rohita roe egg prepared by gastrointestinal proteases
    2015
    Co-Authors: Meram Chalamaiah, T. Jyothirmayi, Prakash V Diwan, Dinesh B Kumar
    Abstract:

    Previously, we have reported the chemical composition, molecular mass distribution and antioxidant activity of rohu roe Protein Hydrolysates. In the current study, antiproliferative, angiotensin-converting enzyme (ACE)-inhibitory activities and functional properties of Protein Hydrolysates from rohu (Labeo rohita) roe Proteins, prepared by gastrointestinal proteases (pepsin and trypsin), were investigated. Antiproliferative activity was evaluated against human colon cancer cell line Caco-2. The results showed that the pepsin hydrolysate possessed dose dependent inhibitory effect on Caco-2 cell line. Pepsin and trypsin Hydrolysates displayed ACE-inhibitory activity in vitro. The ACE-inhibitory activity of the hydrolysate generated by pepsin (47 ± 1.7 %, at 1 mg/ml) is higher than that obtained by trypsin (36 ± 3.2 %). Additionally, the undigested rohu roe Proteins and its Hydrolysates exhibited functional properties. Solubilities of the Hydrolysates were above 81 ± 9.2 % at all pH values tested. Pepsin and trypsin Hydrolysates showed good foaming capacity (45-211 %) and emulsification activity (4-29 m(2)/g). The foaming abilities and emulsifying activity index (EAI) were affected by pH. The results suggest that Protein Hydrolysates from rohu roe could be useful in food industry for various applications.

  • immunomodulatory effects of Protein Hydrolysates from rohu labeo rohita egg roe in balb c mice
    2014
    Co-Authors: Meram Chalamaiah, T. Jyothirmayi, R Hemalatha, Prakash V Diwan, Uday P Kumar, Chetan Nimgulkar, Dinesh B Kumar
    Abstract:

    Protein Hydrolysates prepared from underutilized rohu (Labeo rohita) egg (roe), by enzymatic hydrolysis using pepsin, trypsin and Alcalase, were evaluated for their immunomodulatory effects in BALB/c mice. The female BALB/c mice (4–6 weeks, 18–20 g) were administered with the rohu egg Protein Hydrolysates (REPHs) daily for a period of forty five days with concentration of 0.25, 0.5 and 1 g/kg body weight. Both innate and adaptive immune responses were studied. Pepsin hydrolysate significantly increased the splenic NK cell cytotoxicity, macrophage phagocytosis and level of serum immunoglobulin A (IgA). The mucosal immunity (S-IgA) in the gutwas significantly enhanced by pepsin and Alcalase Hydrolysates.Whereas trypsin hydrolysate induced significant increases in the percentages of CD4+ and CD8+ cells inthe spleen. This study confirms that REPHs are able to modulate immune function and further reveals that different rohu egg Protein Hydrolysates may exert differential influences on the immune system. These results suggest that REPHs contain immunostimulatory peptides that could be useful in pharmaceutical, health food or nutraceutical industry for various applications.

  • fish Protein Hydrolysates proximate composition amino acid composition antioxidant activities and applications a review
    2012
    Co-Authors: Meram Chalamaiah, Dinesh B Kumar, R Hemalatha, T. Jyothirmayi
    Abstract:

    The fish processing industry produces more than 60% by-products as waste, which includes skin, head, viscera, trimmings, liver, frames, bones, and roes. These by-product wastes contain good amount of Protein rich material that are normally processed into low market-value products, such as animal feed, fish meal and fertilizer. In view of utilizing these fish industry wastes, and for increasing the value to several underutilised fish species, Protein Hydrolysates from fish Proteins are being prepared by several researchers all over the world. Fish Protein Hydrolysates are breakdown products of enzymatic conversion of fish Proteins into smaller peptides, which normally contain 2-20 amino acids. In recent years, fish Protein Hydrolysates have attracted much attention of food biotechnologists due to the availability of large quantities of raw material for the process, and presence of high Protein content with good amino acid balance and bioactive peptides (antioxidant, antihypertensive, immunomodulatory and antimicrobial peptides).

  • Protein Hydrolysates from meriga cirrhinus mrigala egg and evaluation of their functional properties
    2010
    Co-Authors: Meram Chalamaiah, Narsing G Rao, D G Rao, T. Jyothirmayi
    Abstract:

    Protein Hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The Protein content of Alcalase-produced hydrolysate was higher (85%) than that of papain hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased Protein solubility of fish egg Protein Hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the Hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g hydrolysate), respectively for Alcalase and papain Protein Hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg Protein Hydrolysates could be useful in the food industry.

T. Jyothirmayi - One of the best experts on this subject based on the ideXlab platform.

  • antiproliferative ace inhibitory and functional properties of Protein Hydrolysates from rohu labeo rohita roe egg prepared by gastrointestinal proteases
    2015
    Co-Authors: Meram Chalamaiah, T. Jyothirmayi, Prakash V Diwan, Dinesh B Kumar
    Abstract:

    Previously, we have reported the chemical composition, molecular mass distribution and antioxidant activity of rohu roe Protein Hydrolysates. In the current study, antiproliferative, angiotensin-converting enzyme (ACE)-inhibitory activities and functional properties of Protein Hydrolysates from rohu (Labeo rohita) roe Proteins, prepared by gastrointestinal proteases (pepsin and trypsin), were investigated. Antiproliferative activity was evaluated against human colon cancer cell line Caco-2. The results showed that the pepsin hydrolysate possessed dose dependent inhibitory effect on Caco-2 cell line. Pepsin and trypsin Hydrolysates displayed ACE-inhibitory activity in vitro. The ACE-inhibitory activity of the hydrolysate generated by pepsin (47 ± 1.7 %, at 1 mg/ml) is higher than that obtained by trypsin (36 ± 3.2 %). Additionally, the undigested rohu roe Proteins and its Hydrolysates exhibited functional properties. Solubilities of the Hydrolysates were above 81 ± 9.2 % at all pH values tested. Pepsin and trypsin Hydrolysates showed good foaming capacity (45-211 %) and emulsification activity (4-29 m(2)/g). The foaming abilities and emulsifying activity index (EAI) were affected by pH. The results suggest that Protein Hydrolysates from rohu roe could be useful in food industry for various applications.

  • immunomodulatory effects of Protein Hydrolysates from rohu labeo rohita egg roe in balb c mice
    2014
    Co-Authors: Meram Chalamaiah, T. Jyothirmayi, R Hemalatha, Prakash V Diwan, Uday P Kumar, Chetan Nimgulkar, Dinesh B Kumar
    Abstract:

    Protein Hydrolysates prepared from underutilized rohu (Labeo rohita) egg (roe), by enzymatic hydrolysis using pepsin, trypsin and Alcalase, were evaluated for their immunomodulatory effects in BALB/c mice. The female BALB/c mice (4–6 weeks, 18–20 g) were administered with the rohu egg Protein Hydrolysates (REPHs) daily for a period of forty five days with concentration of 0.25, 0.5 and 1 g/kg body weight. Both innate and adaptive immune responses were studied. Pepsin hydrolysate significantly increased the splenic NK cell cytotoxicity, macrophage phagocytosis and level of serum immunoglobulin A (IgA). The mucosal immunity (S-IgA) in the gutwas significantly enhanced by pepsin and Alcalase Hydrolysates.Whereas trypsin hydrolysate induced significant increases in the percentages of CD4+ and CD8+ cells inthe spleen. This study confirms that REPHs are able to modulate immune function and further reveals that different rohu egg Protein Hydrolysates may exert differential influences on the immune system. These results suggest that REPHs contain immunostimulatory peptides that could be useful in pharmaceutical, health food or nutraceutical industry for various applications.

  • fish Protein Hydrolysates proximate composition amino acid composition antioxidant activities and applications a review
    2012
    Co-Authors: Meram Chalamaiah, Dinesh B Kumar, R Hemalatha, T. Jyothirmayi
    Abstract:

    The fish processing industry produces more than 60% by-products as waste, which includes skin, head, viscera, trimmings, liver, frames, bones, and roes. These by-product wastes contain good amount of Protein rich material that are normally processed into low market-value products, such as animal feed, fish meal and fertilizer. In view of utilizing these fish industry wastes, and for increasing the value to several underutilised fish species, Protein Hydrolysates from fish Proteins are being prepared by several researchers all over the world. Fish Protein Hydrolysates are breakdown products of enzymatic conversion of fish Proteins into smaller peptides, which normally contain 2-20 amino acids. In recent years, fish Protein Hydrolysates have attracted much attention of food biotechnologists due to the availability of large quantities of raw material for the process, and presence of high Protein content with good amino acid balance and bioactive peptides (antioxidant, antihypertensive, immunomodulatory and antimicrobial peptides).

  • Protein Hydrolysates from meriga cirrhinus mrigala egg and evaluation of their functional properties
    2010
    Co-Authors: Meram Chalamaiah, Narsing G Rao, D G Rao, T. Jyothirmayi
    Abstract:

    Protein Hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The Protein content of Alcalase-produced hydrolysate was higher (85%) than that of papain hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased Protein solubility of fish egg Protein Hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the Hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g hydrolysate), respectively for Alcalase and papain Protein Hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg Protein Hydrolysates could be useful in the food industry.

  • Protein Hydrolysates from meriga cirrhinus mrigala egg and evaluation of their functional properties
    2010
    Co-Authors: Meram Chalamaiah, T. Jyothirmayi
    Abstract:

    Protein Hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The Protein content of Alcalase-produced hydrolysate was higher (85%) than that of papain hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased Protein solubility of fish egg Protein Hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the Hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g hydrolysate), respectively for Alcalase and papain Protein Hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg Protein Hydrolysates could be useful in the food industry.

Abraham T Girgih - One of the best experts on this subject based on the ideXlab platform.

  • enzymatic Protein Hydrolysates from high pressure pretreated isolated pea Proteins have better antioxidant properties than similar Hydrolysates produced from heat pretreatment
    2015
    Co-Authors: Abraham T Girgih, Dongfang Chao, Lin Lin, Stephanie Jung, Rotimi E. Aluko
    Abstract:

    Isolated pea Protein (IPP) dispersions (1%, w/v) were pretreated with high pressure (HP) of 200, 400, or 600 MPa for 5 min at 24 °C or high temperature (HT) for 30 min at 100 °C prior to hydrolysis with 1% (w/w) Alcalase. HP pretreatment of IPP at 400 and 600 MPa levels led to significantly (P 40%) oxygen radical absorption capacity (ORAC) of Hydrolysates. 2,2-Diphenyl-1-picrylhydrazyl, superoxide radical and hydroxyl radical scavenging activities of pea Protein Hydrolysates were also significantly (P<0.05) improved (25%, 20%, and 40%, respectively) by HP pretreatment of IPP. Protein Hydrolysates from HT IPP showed no ORAC, superoxide or hydroxyl scavenging activity but had significantly (P<0.05) improved (80%) ferric reducing antioxidant power. The Protein Hydrolysates had weaker antioxidant properties than glutathione but overall, the HP pretreatment was superior to HT pretreatment in facilitating enzymatic release of antioxidant peptides from IPP.

  • structural and antihypertensive properties of enzymatic hemp seed Protein Hydrolysates
    2015
    Co-Authors: Sunday A Malomo, Abraham T Girgih, John O Onuh, Rotimi E. Aluko
    Abstract:

    The aim of this work was to produce antihypertensive Protein Hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed Proteins (HSP). The hemp seed Protein Hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed Protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

  • structural and antihypertensive properties of enzymatic hemp seed Protein Hydrolysates
    2015
    Co-Authors: Sunday A Malomo, Abraham T Girgih, John O Onuh, Rotimi E. Aluko
    Abstract:

    The aim of this work was to produce antihypertensive Protein Hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed Proteins (HSP). The hemp seed Protein Hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed Protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

  • blood pressure lowering effects of australian canola Protein Hydrolysates in spontaneously hypertensive rats
    2014
    Co-Authors: Abraham T Girgih, Sunday A Malomo, Adeola M Alashi, Christopher Blanchard, Rodney J Mailer, Samson Agboola, A J Mawson, Rotimi E. Aluko
    Abstract:

    Abstract The in vitro and in vivo antihypertensive activities of canola Protein Hydrolysates and ultrafiltration membrane fractions (

  • antioxidant activities of enzymatic rapeseed Protein Hydrolysates and the membrane ultrafiltration fractions
    2013
    Co-Authors: Abraham T Girgih, Sunday A Malomo, Rong He, Xingrong Ju, Rotimi E. Aluko
    Abstract:

    In this study, rapeseed Protein isolate was hydrolyzed with various proteases to obtain Hydrolysates that were separated by membrane ultrafiltration into four molecular size fractions (<1, 1–3, 3–5, and 5–10 kDa). Alcalase hydrolysis significantly (p < 0.05) produced the highest yield of Protein hydrolysate while Flavourzyme produced the least. The <1 kDa fraction was the most abundant after the membrane ultrafiltration of the Protein Hydrolysates, which indicates that the proteases were efficient at reducing the native rapeseed Proteins into low molecular weight peptides. Antioxidant properties of the resulting Hydrolysates and membrane fractions were characterized and results showed the Pepsin + Pancreatin (P + P) Protein hydrolysate had significantly highest (p < 0.05) scavenging activity against DPPH radical among the unfractionated enzymatic Hydrolysates. But the P + P hydrolysate was not as effective as other Hydrolysates during long-term inhibition of linoleic acid oxidation. For most of the samples, fractionation into the <1 kDa peptides significantly (p < 0.05) improved DPPH and superoxide scavenging properties when compared to the unfractionated Protein Hydrolysates. Only the <1 kDa fraction showed ferric reducing antioxidant power and the effect was dose-dependent. Overall, Alcalase and Proteinase K seem to be more efficient proteases to release antioxidant peptides from rapeseed Proteins when compared to P + P, Flavourzyme and Thermolysin.

Sunday A Malomo - One of the best experts on this subject based on the ideXlab platform.

  • structural and antihypertensive properties of enzymatic hemp seed Protein Hydrolysates
    2015
    Co-Authors: Sunday A Malomo, Abraham T Girgih, John O Onuh, Rotimi E. Aluko
    Abstract:

    The aim of this work was to produce antihypertensive Protein Hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed Proteins (HSP). The hemp seed Protein Hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed Protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

  • structural and antihypertensive properties of enzymatic hemp seed Protein Hydrolysates
    2015
    Co-Authors: Sunday A Malomo, Abraham T Girgih, John O Onuh, Rotimi E. Aluko
    Abstract:

    The aim of this work was to produce antihypertensive Protein Hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed Proteins (HSP). The hemp seed Protein Hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed Protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

  • blood pressure lowering effects of australian canola Protein Hydrolysates in spontaneously hypertensive rats
    2014
    Co-Authors: Abraham T Girgih, Sunday A Malomo, Adeola M Alashi, Christopher Blanchard, Rodney J Mailer, Samson Agboola, A J Mawson, Rotimi E. Aluko
    Abstract:

    Abstract The in vitro and in vivo antihypertensive activities of canola Protein Hydrolysates and ultrafiltration membrane fractions (

  • antioxidant activities of enzymatic rapeseed Protein Hydrolysates and the membrane ultrafiltration fractions
    2013
    Co-Authors: Abraham T Girgih, Sunday A Malomo, Rong He, Xingrong Ju, Rotimi E. Aluko
    Abstract:

    In this study, rapeseed Protein isolate was hydrolyzed with various proteases to obtain Hydrolysates that were separated by membrane ultrafiltration into four molecular size fractions (<1, 1–3, 3–5, and 5–10 kDa). Alcalase hydrolysis significantly (p < 0.05) produced the highest yield of Protein hydrolysate while Flavourzyme produced the least. The <1 kDa fraction was the most abundant after the membrane ultrafiltration of the Protein Hydrolysates, which indicates that the proteases were efficient at reducing the native rapeseed Proteins into low molecular weight peptides. Antioxidant properties of the resulting Hydrolysates and membrane fractions were characterized and results showed the Pepsin + Pancreatin (P + P) Protein hydrolysate had significantly highest (p < 0.05) scavenging activity against DPPH radical among the unfractionated enzymatic Hydrolysates. But the P + P hydrolysate was not as effective as other Hydrolysates during long-term inhibition of linoleic acid oxidation. For most of the samples, fractionation into the <1 kDa peptides significantly (p < 0.05) improved DPPH and superoxide scavenging properties when compared to the unfractionated Protein Hydrolysates. Only the <1 kDa fraction showed ferric reducing antioxidant power and the effect was dose-dependent. Overall, Alcalase and Proteinase K seem to be more efficient proteases to release antioxidant peptides from rapeseed Proteins when compared to P + P, Flavourzyme and Thermolysin.

Related terms

Protein Hydrolysates - 15 days free trial to Access Experts & Abstracts