Some studies on the protease from a novel source: The plantCucurbita ficifolia

Illanes, Andrés; Schaffeld, G.; Schiappacasse, C.; Zúñiga, Marı́a Elvira; González, Gustavo; Curotto, E.; Tapia, Guillermina; O'Reilly, Sybil

doi:10.1007/bf01040207

Cited by 8 publications

(2 citation statements)

References 1 publication

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“…Whey proteins are significantly resistant to hydrolysis and the use of enzymes significantly increases the cost of their production. One of the promising alternatives is the use of plant serine protease isolated from C. ficifolia, exhibiting attractive proteolytic properties towards casein, protein from corn gluten meal (CGM) or ovoalbumin (Illanes et al 1985 ; Curotto et al 1989 ; Pokora et al 2014 ). The protease exhibits a very high and broad pH optimum with a maximum at 10.7 and is able to cleave four bonds in an endogenous serine proteinase inhibitor.…”

Section: Introductionmentioning

confidence: 99%

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)

Babij

Dąbrowska

Szołtysik

et al. 2014

Int J Pept Res Ther

107

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In the present study, whey protein concentrate (WPC-80) and β-lactoglobulin were hydrolyzed with a noncommercial serine protease isolated from Asian pumpkin (Cucurbita ficifolia). Hydrolysates were further fractionated by ultrafiltration using membranes with cut-offs equal 3 and 10 kDa. Peptide fractions of molecular weight lower than 3 and 3–10 kDa were further subjected to the RP-HPLC. Separated preparations were investigated for their potential as the natural inhibitors of dipeptidyl peptidase (DPP-IV), α-glucosidase and angiotensin converting enzyme (ACE). WPC-80 hydrolysate showed higher inhibitory activities against the three tested enzymes than β-lactoglobulin hydrolysate. Especially high biological activities were exhibited by peptide fractions of molecular weight lower than 3 kDa, with ACE IC50 <0.64 mg/mL and DPP-IV IC50 <0.55 mg/mL. This study suggests that peptides generated from whey proteins may support postprandial glycemia regulation and blood pressure maintenance, and could be used as functional food ingredients in the diet of patients with type 2 diabetes.

show abstract

Section: Introductionmentioning

confidence: 99%

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)

Babij

Dąbrowska

Szołtysik

et al. 2014

Int J Pept Res Ther

107

View full text Add to dashboard Cite

show abstract

“…For example, plant serine protease isolated from C. ficifolia fruit exhibits attractive proteolytic properties which have been analyzed towards e.g. casein or protein from corn gluten meal (CGM) (Illanes et al 1985 ; Curotto et al 1989 ).…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein

et al. 2015

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In the present study the effect of hydrolysis with non-commercial Cucurbita ficifolia serine protease on a reduction of the IgE and IgG binding capacity of whey protein concentrate and αs-casein was investigated. The intensity of the protein degradation was analyzed by the degree of hydrolysis, the free amino groups content and RP-HPLC. The ability to bind the antibodies by native proteins and their hydrolysates was determined using a competitive ELISA test. Deep hydrolysis contributed to a significant reduction of immunoreactive epitopes present in WPC. In the case of IgE and IgG present in the serum pool of children with CMA, the lowest binding capacity was detected in the 24 h WPC hydrolysate, where the inhibition of the reaction with native WPC was ≤23 and ≤60 %, respectively. The analysis of the IgG reactivity in the antiserum of the immunized goat showed that the lowest antibody binding capacity was exhibited also by 24 h WPC hydrolysate at a concentration of 1000 μg/ml where the inhibition of the reaction with nWPC was ≤47 %. One-hour hydrolysis of α-casein was sufficient to significant reduction of the protein antigenicity, while the longer time (5 h) of hydrolysis probably lead to the appearance of new epitopes reactive with polyclonal.

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Pumpkins, Squashes, and Gourds (Cucurbita L.) of North America

Kates

2019

North American Crop Wild Relatives, Volume 2

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Some studies on the protease from a novel source: The plantCucurbita ficifolia

Cited by 8 publications

References 1 publication

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)

Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein

Pumpkins, Squashes, and Gourds (Cucurbita L.) of North America

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