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PubMed1994

Metabolic balance studies and plasma amino acid concentrations in preterm infants fed experimental protein hydrolysate preterm formulas.

The aim of this study was to investigate absorption and retention of nitrogen, fat, calcium, phosphorus and magnesium, as well as plasma amino acid concentrations in 19 preterm infants fed three experimental protein hydrolysate preterm formulas (PTHF): seven received a preterm formula based on 100% whey hydrolysate protein (PTHF1), seven other infants were fed a preterm formula based on a mixture of 78% whey and 22% casein hydrolysed protein (PTHF2) and a third group of five infants were fed the same type of protein hydrolysate (78/22) enriched with histidine (PTHF3). Metabolic balances (n = 39) and plasma amino acid concentrations (n = 12) in preterm infants fed a standard preterm formula (whey/casein: 60/40) were included as a control group. Amino acid composition of the formulas was determined after complete hydrolysis with 12 N HCl. Compared with the standard preterm formula, the use of protein hydrolysate formulas led to a decrease in nitrogen and phosphorus absorption without modification of retention. Net absorption of calcium and magnesium was not significantly different in the four groups but calcium intake necessary to obtain calcium retention similar to the standard preterm formula was higher in the infants fed the hydrolysate formulas. Plasma amino acid concentrations were related to the amino acid composition of the formulas. Compared with the standard preterm formula, all three protein hydrolysate formulas led to a significant increase in plasma threonine, and a decrease in tyrosine and phenylalanine concentrations. In addition, there was an important reduction in plasma histidine concentrations with PTHF1.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMed2026

Functional and Nutritional Potential of Chickpea Protein Hydrolysates: A Systematic Review and Plant-protein Network Analysis.

Chickpea is a protein-rich legume increasingly explored as a substrate for functional plant-based ingredients. Chickpea protein hydrolysates (CPHs) and chickpea-derived peptides (CPs), obtained through enzymatic hydrolysis or simulated gastrointestinal digestion, may provide technological and biological properties while supporting the valorization of chickpea fractions and by-products. This review integrates a network analysis of title-abstract terms from 5,728 unique Scopus and PubMed records on plant protein hydrolysates with a systematic review of 72 studies focused on CPH production, peptide characterization, bioactivity, and translational gaps. The evidence indicates that CPHs and CPs show promising antioxidant, antihypertensive, antidiabetic, anti-inflammatory, lipid-lowering, immunomodulatory, antimicrobial, and anticancer-related activities, mainly supported by biochemical assays, cell models, and animal studies. However, heterogeneous hydrolysis protocols, incomplete peptide characterization, inconsistent bioactivity methods, limited scale-up evidence, and the absence of human intervention trials restrict translation. Future studies should prioritize standardized protocols, mechanistic validation, bioavailability, sensory and regulatory assessment, food-matrix validation, and clinical trials.

Cicer↗
PubMed1995

Evaluation by SDS-PAGE and immunoblotting of residual antigenicity in hydrolysed protein formulas.

BACKGROUND: Extensively hydrolysed protein formulas are widely used as an alternative diet for children with cow's milk allergy. Partially hydrolysed protein formulas have been noted in some studies as useful in the prevention of allergy in infants at high risk of atopy. Although normally well tolerated, these 'hypoallergenic' products have been reported to cause serious immunological reactions in very sensitive subjects. OBJECTIVE: Starting from these considerations, we studied some commercial hydrolysed formulas in search of biological data supporting the observed clinical reactions. METHODS: We set up an electrophoretic method sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) which allowed us to study the molecular weight of peptides contained in hydrolysed products. Then, using the immunoblotting technique we evaluated the reactivity of circulating IgE (from serum of children allergic to cow's milk proteins) with the residual intact proteins and with the peptides present in these formulas. RESULTS: Both group of milk proteins (caseins and whey proteins) were important allergens for children included in this study. The presence of high-molecular polypeptides was shown in partial hydrolysed formulas as such and in extensive hydrolysed products after protein enrichment by trichloroacetic acid (TCA) precipitation. Intact residual proteins were mainly responsible for the formation of IgE-antigen complexes observed in immunoblotting. More rarely, polypeptides of partial hydrolysed formulas were involved in immunological responses. CONCLUSIONS: Both partial and extensive hydrolysed formulas could induce clinical reactions in very sensitive subjects. These responses are mainly associated with allergy to the small amounts of residual intact proteins.

Animals↗
PubMed2006

Utilization of meat industry by products: protein hydrolysate from sheep visceral mass.

Protein hydrolysate was prepared from pre-treated sheep visceral mass (including stomach, large and small intestines) by enzymatic treatment at 43+/-1 degrees C (at the in situ pH 7.1+/-0.2 of the visceral mass) using fungal protease. The enzyme readily solubilized the proteins of the visceral mass as indicated by the degree of hydrolysis (34%) and nitrogen recovery (>64%). Hydrolysis with an enzyme level of 1% (w/w of total solids) at 43+/-1 degrees C with a pH around 7.0 for 45 min was found to be the optimum condition. The yield of protein hydrolysate was about 6% (w/w). The amino acid composition of the protein hydrolysate that was very hygroscopic, was comparable to that of casein.

Animals↗
PubMed1996

[Protein hydrolysates in infant formulas].

The paper describes protein hydrolysates methods of hydrolysis, classification of hydrolysates based on the type of hydrolysed protein and extent of hydrolysis, conditions which should be fulfilled to ensure the hypoallergenicity (hypoantigenicity) of hydrolysed formulae. The indications for use in treatment and prevention are discussed.

Child, Preschool↗
PubMed1999

Production of extensive chickpea (Cicer arietinum L.) protein hydrolysates with reduced antigenic activity.

Chickpea protein isolate was used as starting material for the production of hypoallergenic protein hydrolysates. Western blotting of the protein isolate showed that IgE in sensitized patient sera strongly bound to the basic polypeptidic chains and recognized the acidic ones of 11S globulin. During the hydrolysis process by the individual and/or sequential action of endo- and exoproteases, a high reduction of antigenic activity was observed. Results suggest that the presence of intact or partially hydrolyzed basic polypeptide chains of 11S globulin are responsible for the formation of IgE complexes in protein hydrolysates obtained by exoprotease treatment; however, the digestion of these polypeptide chains by individual action of endoprotease caused a high loss of antigenic activity. The most effective reduction of antigenicity, >90%, was observed in extensive hydrolyzed chickpea proteins obtained by sequential treatment with endo- and exopeptidases. This chickpea protein hydrolysate could be useful for the elaboration of specialized hypoallergenic food products.

Blotting, Western↗
PubMedDate not supplied

Structural modulation of calmodulin and calmodulin-dependent protein kinase II by pea protein hydrolysates.

The effects of two fractions of pea protein hydrolysate with high levels of positively charged amino acids on the structural conformations of calmodulin (CaM) and CaM-dependent protein kinase II (CaMKII) were determined using fluorescence and circular dichroism methods. In the presence of Ca2 + , addition of the protein hydrolysates to CaM and CaM/CaMKII complex led to increased exposure of aromatic groups as measured by intrinsic and extrinsic fluorescence spectroscopy. Near-UV circular dichroism data revealed an increase in the tertiary structure of CaM in the presence of pea protein hydrolysates. Effect of the protein hydrolysates on the CaM structure was greater with the fraction that contained higher contents of arginine and lysine when compared with the fraction with lower levels of these two amino acids. We concluded that the presence of the pea protein hydrolysates led to rearrangement of the native protein structure and exposure of buried hydrophobic groups of CaM and/or CaMKII.

Calcium-Calmodulin-Dependent Protein Kinase Type 2↗
PubMed1999

[Allergy to cow's milk protein hydrolysates: apropos of 8 cases].

BACKGROUND: The use of extensively hydrolyzed protein formulas is the best alternative for children with cow's milk allergy, though cases of allergies to hydrolyzed proteins have been reported. The aim of this study was to clarify from our experience the diagnostic, evolutive and therapeutic aspects of allergies to extensively hydrolyzed protein formulas. PATIENTS AND METHODS: We report eight cases of allergy to extensively hydrolyzed protein formulas seen between 1985 and 1998. The diagnostic criteria for allergy were either the appearance of immediate anaphylactic reactions after the ingestion of protein hydrolysate or a positive challenge test with the protein hydrolysate. RESULTS: Four children developed immediate anaphylactic symptoms after ingesting protein hydrolysate, and four children demonstrated subacute or chronic gastrointestinal symptoms. All children who developed acute anaphylactic symptoms had positive skin tests and specific IgF, antibodies (RAST) to cow's milk and/or hydrolyzed proteins. Conversely, in the four children with chronic gastrointestinal symptoms, skin tests and specific IgE antibodies were negative in three cases, but intestinal histology was abnormal in all of them when they were fed with a protein hydrolysate; this became normal after excluding the hydrolysate (data available in only two cases). Three children tolerated another protein hydrolysate form (whey vs. casein), four children had a favourable outcome when fed with human milk, and an amino-acid-based formula was successfully used in the most recent case. Nonhydrolyzed cow's milk proteins were tolerated after the age of 18 months in six children. Other atopic symptoms were observed in six children. CONCLUSION: Allergy to cow's milk protein hydrolysate is rare. The diagnosis is usually easy in children who develop acute anaphylactic symptoms, though intestinal histology is generally necessary for the diagnosis of allergy with chronic gastrointestinal symptoms. Treatment is based on the use of either another protein hydrolysate form (whey vs. casein) or an amino-acid-based formula.

Age Factors↗
PubMed2000

Inhibitory effect of protein hydrolysates on calcium carbonate crystallization.

Protein hydrolysates, prepared by enzymatic digestion of soybean protein and egg white albumin using several proteases, inhibited the crystal growth of calcium carbonate. Each hydrolysate showed different inhibitory activities, suggesting the key role of peptide structures in the inhibition. The deamidation of protein hydrolysates by glutaminase increased not only the inhibitory activity toward the crystal growth of calcium carbonate but also the resistance of the hydrolysates against peptic digestion. Furthermore, the addition of sodium chloride, citric acid, or lactose into the reaction mixture enhanced the inhibitory activity. The protein hydrolysates inhibited both nucleation and crystal growth of calcium carbonate and also affected the crystal morphology.

Calcium Carbonate↗
PubMed1985

Net protein utilization determined by rat bioassay of a protein hydrolysate and a diet for children with phenylketonuria.

In a previous study (Kindt et al. 1983, 1984) it was assumed that a protein hydrolysate, devoid of phenylalanine, together with intact protein as given to children with phenylketonuria (PKU), was equivalent to egg or milk protein. One group of children was given this 'PKU protein' in amounts corresponding to the Joint FAO/WHO ad hoc Expert Committee (1973) recommendations. The results indicated that the Joint FAO/WHO ad hoc Expert Committee (1973) recommended levels of protein intake were marginal. The purpose of the present study was to evaluate whether the quality of the protein hydrolysate, together with intact protein ('PKU protein'), is equivalent to egg or milk protein. This was done using a rat bioassay. Four protein sources were used: (1) egg protein, (2) protein hydrolysate, (3) protein hydrolysate diluted with non-essential amino acids, (4) protein hydrolysate mixed with food proteins ('PKU protein'), comparable with the diet previously used (Kindt et al. 1983, 1984). The results indicated that the 'PKU protein' was of very high quality: net protein utilization (NPU) greater than 90. The protein hydrolysate alone and the protein hydrolysate diluted with non-essential amino acids gave a NPU greater than 80. The conclusion drawn from the present study is that the 'PKU protein', as used in the treatment of children with PKU, is equivalent to egg or milk protein. This supported the view that the Joint FAO/WHO ad hoc Expert Committee (1973) recommended levels of intake were marginal.

Animals↗
PubMed1985

Comparative effects of protein, protein hydrolysate and amino acid diets on nitrogen metabolism of normal, protein-deficient, gastrectomized or hepatectomized rats.

The effects of diets containing protein, protein hydrolysate or an amino acid mixture on nitrogen metabolism of normal and severely protein-deficient rats and on rats after gastrectomy and hepatectomy were compared. In experiment 1, rats weighing about 80 g were fed one of three experimental diets containing casein, protein hydrolysate or an amino acid mixture for 28 d. In experiment 2, rats weighing about 270 g were fed a protein-free diet for 40 d, and then one of the above three experimental diets for 14 d. In experiment 3, rats weighing about 220 g were totally gastrectomized and fed one of the three experimental diets for 21 d. In experiment 4, rats weighing about 210 g had about 70% of the liver resected, and then were fed one of the three experimental diets for 15 d. In all four experiments, daily food intake, daily body weight gain, nitrogen balance, urinary nitrogen compounds, body composition and hematologic values were measured. In normal, protein-deficient and hepatectomized rats, most results were similar for the groups fed protein, protein hydrolysate or amino acid diets, except that urinary ammonia was higher in the group fed the amino acid diet than in the other two groups. For about 10 d after total gastrectomy, food intake and growth of the animals fed the protein diet were lower than in the other two groups.

Amino Acids↗
PubMed2006

Usability of size-excluded fractions of soy protein hydrolysates for growth and viability of Chinese hamster ovary cells in protein-free suspension culture.

To investigate the effect of size-excluded fraction of non-animal protein hydrolysate on growth, viability and longevity of Chinese hamster ovary (CHO) cells, several commercially available protein hydrolysates were evaluated as a feed supplement to chemically-defined protein-free suspension culture. Soy protein hydrolysates showed better supporting capability for cell growth and viability than the other types of hydrolysates. Maximal cell growth was not affected greatly by size exclusion of some soy hydrolysates such as bacto soytone and soy hydrolysates. CHO cells supplemented with size-excluded fractions of the two hydrolysates showed viable cell density and viability almost equal to those with their crude hydrolysates, although soy hydrolysates showed a little better performance. This suggested that the size-excluded hydrolysate fractions of some soy hydrolysate might be a potential culture medium additive to achieve better downstream operation in a large-scale production as well as enhanced productivity.

Animals↗
PubMed1992

Detection and possible origins of aminomalonic acid in protein hydrolysates.

Aminomalonic acid (Ama) was first detected in alkaline hydrolysates of proteins in 1984. In this work we describe our search for the origin of aminomalonic acid in alkaline hydrolysates of proteins. We have developed a technique for quantitation of aminomalonic acid based upon gas chromatography/mass spectrometry. Using this technique, we find approximately 0.3 Ama/1000 amino acids in hydrolysates of Escherichia coli protein. We have demonstrated that Ama is not formed from any of the 20 major amino acids during the hydrolysis procedure. Furthermore, the amount of Ama found does not depend on the presence of small amounts of O2 during the hydrolysis. Thus far, we have not been able to demonstrate an artifactual origin for Ama. The results described above suggest that Ama may indeed be a constituent of proteins before the hydrolysis procedure. Possible origins of Ama include errors in protein synthesis and oxidative damage to amino acid residues in proteins.

Amino Acid Sequence↗
PubMed1978

Chlorohydrins in protein hydrolysates.

Four samples of neutral fractions of protein hydrolysates were separated by gas chromatography and the individual components were identified from the mass spectra obtained. Some of the identified compounds were not previously reported as volatile components of foodstuffs. Three of these compounds namely 3-chloropropan-1-ol, 2,3-dichloropropan-1-ol, and 1,3-dichloropropan-2-ol, were toxic chlorohydrins. 1,3-Dichloropropan-2-ol was present in samples in concentrations 0.17 to 0.94 mg/kg. To check the possibilities of the formation of these chlorohydrins and to find their precursor, glycerol, and hydrochloric acid mixtures were heated under conditions of producing protein hydrolysates. All three chlorohydrins, formerly found in protein hydrolysates have been identified.

Chlorohydrins↗
PubMedDate not supplied

[Characteristics and use of protein hydrolysates (review)].

Properties of protein hydrolysates and possible uses of these substances in research and various branches of industry are considered. The main problem discussed in this paper is the relationship between the degree of protein conversion and characteristics (structural-functional and physicochemical) of hydrolysates.

Protein Hydrolysates↗
PubMed1998

Contact urticaria from protein hydrolysates in hair conditioners.

Protein hydrolysates (PHs) are added to hair-care products (to "repair" broken hair), soaps, bath gels, creams, etc. From one to 22 PHs used in hair-care products (collagen, keratin, elastin, milk, wheat, almond, and silk) were tested in three patient groups: A) 11 hairdressers with hand dermatitis B) 2160 consecutive adults with suspected allergic respiratory disease subjected to routine skin prick tests C) 28 adults with atopic dermatitis. In group A, all the 22 PHs were tested with scratch and patch tests. In groups B and C, one to three PHs were tested with prick tests. Positive scratch/prick test reactions were seen in 12 patients from three PHs altogether. All were women with atopic dermatitis, and all reacted to at least hydroxypropyl trimonium hydrolyzed collagen (Crotein Q). In three patients, prick and open tests with a hair conditioner containing Crotein Q were performed with positive results. One patient reported contact urticaria on her hands, and two reported acute urticaria on their head, face, and upper body from a hair conditioner containing Crotein Q. In seven of the eight studied sera, specific IgE to Crotein Q was detected. In conclusion, PHs of hair cosmetics can cause contact urticaria, especially in patients with atopic dermatitis.

Adolescent↗