Tolerogenic mechanisms elicited by extensively hydrolysed casein formula with L. rhamnosus GG

2016 ◽  
Vol 48 ◽  
pp. e277
Author(s):  
L. Paparo ◽  
R. Nocerino ◽  
R. Aitoro ◽  
A. Amoroso ◽  
C. Di Scala ◽  
...  
Keyword(s):  
Hydrolysed Casein

Equivalent Increases in Circulating GLP-1 Following Jejunal Delivery of Intact and Hydrolysed Casein: Relevance to Satiety Induction Following Bariatric Surgery

2015 ◽  
Vol 26 (8) ◽  
pp. 1851-1858 ◽  
Author(s):  
Carel W. le Roux ◽  
My Engström ◽  
Niclas Björnfot ◽  
Lars Fändriks ◽  
Neil G. Docherty
Keyword(s):  
Bariatric Surgery ◽  
Hydrolysed Casein

scholarly journals Endogenous amino acid flow in the avian ileum: quantification using three techniques

2004 ◽  
Vol 92 (2) ◽  
pp. 217-223 ◽  
Author(s):  
V. Ravindran ◽  
L. I. Hew ◽  
G. Ravindran
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Broiler Chickens ◽  
Sole Source ◽  
Physiological Conditions ◽  
Method Of Determination ◽  
Endogenous Protein ◽  
Protein Free Diet ◽  
Hydrolysed Casein ◽  
Endogenous Amino Acid

The aim of the present study was to compare the protein-free diet, guanidinated casein (GuC) and enzyme hydrolysed casein (EHC) methods for the quantification of endogenous amino acid (AA) flow in the avian ileum. Growing broiler chickens (5 weeks old) were used. All three assay diets were based on dextrose, and in the GuC and EHC diets GuC or EHC were the sole source of N. Endogenous AA flows determined with the use of protein-free diet were considerably lower (P>0·05) than those determined by the GuC and EHC methods. The total endogenous AA flows determined by the GuC and EHC methods were almost 3-fold greater (P>0·05) than those determined by the protein-free diet. The endogenous AA values obtained from GuC and EHC methods were similar (P<0·05), except for the flow of arginine, which was lower (P>0·05) in the EHC method. Glutamic acid, aspartic acid, threonine and glycine were the predominant endogenous AA present in digesta from the distal ileum. The contents of methionine, histidine and cystine were lower compared with other AA. The method of determination had no effect on the AA composition of endogenous protein, except for threonine, glutamic acid, lysine, arginine and cystine. The concentrations of threonine and arginine were lower (P>0·05) and that of lysine was higher (P>0·05) with the EHC method compared with the other two methods. The concentration of glutamic acid was greater (P0·05) and that of cystine was lower (P>0·05) in the EHC and GuC methods compared with the protein-free diet method. The results showed that the ileal endogenous flows of N and AA are markedly enhanced by the presence of protein and peptides, above those determined following feeding of a protein-free diet. It is concluded that the use of EHC and GuC methods enables the measurement of ileal endogenous losses in chickens under normal physiological conditions.

scholarly journals Partial purification and characterization of a novel neutral proteinase from human uterine cervix

1980 ◽  
Vol 185 (2) ◽  
pp. 443-450 ◽  
Author(s):  
Akira Ito ◽  
Hiroko Ihara ◽  
Yo Mori
Keyword(s):  
Uterine Cervix ◽  
Gel Filtration ◽  
Reaction System ◽  
Partial Purification ◽  
High Concentration ◽  
Neutral Proteinase ◽  
Bean Trypsin Inhibitor ◽  
Cervical Stroma ◽  
High Concentrations ◽  
Hydrolysed Casein

1. Human uterine cervical stroma was found to contain a Ca2+-independent neutral proteinase against casein and N-benzoyl-dl-arginine p-nitroanilide (Bz-dl-Arg-Nan). This enzyme was tightly bound to an insoluble material (20000g pellet) and was solubilized by high concentrations of NaCl or KCl. High concentrations of them in the reaction system, however, inhibited reversibly the activity of this enzyme. 2. The neutral proteinase was partially purified by extraction with NaCl, gel filtration on Sephadex G-200 and affinity chromatography on casein–Sepharose. 3. The optimal pH of this partially purified enzyme was 7.4–8.0 against casein and Bz-dl-Arg-Nan. The molecular weight of the enzyme was found to be about 1.4×105 by gel filtration on Sephadex G-200. 4. The enzyme was significantly inhibited by di-isopropyl phosphorofluoridate (0.1mm). High concentration of phenylmethanesulphonyl fluoride (5mm), 7-amino-1-chloro-3-l-tosylamidoheptan-2-one (0.5mm), antipain (10μm) or leupeptin (10μm) was also found to be inhibitory, but chymostatin (40μg/ml), soya-bean trypsin inhibitor (2.5mg/ml), human plasma (10%, v/v), p-chloromercuribenzoate (1mm), EDTA (10mm) and 1-chloro-4-phenyl-3-l-tosylamidobutan-2-one (1mm) had no effect on the enzyme. 5. The neutral proteinase hydrolysed casein, Bz-dl-Arg-Nan and heat-denatured collagen, but was inactive towards native collagen and several synthetic substrates, such as 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-d-Arg, 3-carboxypropionyl-Ala-Ala-Ala p-nitroanilide and 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-d-Arg, and also proteoglycan. The enzyme did not act as a plasminogen activator. 6. These properties suggested that a neutral proteinase in the human uterine cervix was different from enzymes previously reported.

Identification of Casein Phosphopeptides in β-casein and Commercial Hydrolysed Casein by Mass Spectrometry

2006 ◽  
Vol 12 (5) ◽  
pp. 379-384 ◽  
Author(s):  
E. Miquel ◽  
J. A. Gómez ◽  
A. Alegría ◽  
R. Barberá ◽  
R. Farré ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Capacity ◽  
Amino Acid Sequences ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
Casein Phosphopeptides ◽  
Hydrolysed Casein ◽  
Cluster Sequence

Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation tandem mass spectrometry (RP-HPLC-ESIMS/MS). In β-CN digest five peptides that contained four to five phosphate groups and the cluster sequence SpSpSpEE (residues 17-21) were identified. All CPPs with one exception β-CN(1-24)4P, had the protein fragment β-CN(1-25)4P, which is one of the main CPPs produced in vivo digestion of casein and the results of in vitro studies showed that this fragment enhanced calcium, iron and zinc absorption. In commercial hydrolysed casein CE90CPP 13 peptides were identified, only one of them, αs2-CN (1-13)3P, contained the cluster sequence SpSpSpEE but all the peptides have one or two phosphoserine residues with mineral binding capacity. These CPPs were shorter (527-2061 Da vs 2966-6512 Da) and less phosphorylated (1-3 P vs 4-5 P) than those released after simulated gastrointestinal digestion of β-CN. In both samples, the potential mineral chelating properties of these peptides in relation to their amino acid sequences and the presence of the phosphorylated cluster are discussed.

scholarly journals Quantitative studies on nitrogen metabolism in the bovine rumen

1972 ◽  
Vol 27 (2) ◽  
pp. 261-283 ◽  
Author(s):  
J. L. Mangan
Keyword(s):  
Amino Acids ◽  
Half Life ◽  
Rumen Fluid ◽  
Casein Hydrolysate ◽  
Maximum Amount ◽  
Quantitative Studies ◽  
Monozygous Twin ◽  
The Individual ◽  
Hydrolysed Casein ◽  
Standard Ration

1. Monozygous twin cattle with permanent rumen fistulas were used to measure the rate of degradation of casein and ovalbumin. One twin was used as a control and the other had protein administered by fistula about 4.75 h after eating a standard ration.2. Casein was rapidly degraded with a half-life in the range 5.6–21.5 min, with the formation of peptides, free amino acids and finally ammonia. Up to 43% of the casein nitrogen was found as ammonia in the rumen fluid. Most of the amino acids present in casein were found in the free state in the rumen fluid to an extent of less than 7%, but valine, leucine, isoleucine and lysine were present as 25, 27, 21 and 38% respectively of the amounts present in the casein administered.3. When acid-hydrolysed casein was given, ammonia was rapidly formed, the maximum amount found in the rumen being equivalent to 39% of the casein N. The individual amino acids were rapidly broken down except for valine, leucine, isoleucine and lysine of which synthesis in addition to degradation may occur.4. Ovalbumin was degraded slowly with a half-life of 175 min, which was reduced to 132 min by feeding the cattle with ovalbumin for 5 d. Ammonia was produced slowly.5. When added together the two proteins were degraded in the rumen independently at their own rates.6. δ-Amino-n-valeric acid was produced in large quantity when casein or casein hydrolysate was degraded in the rumen.

scholarly journals Infectivity ofPasteurella tularensisclouds

1961 ◽  
Vol 59 (4) ◽  
pp. 497-504 ◽  
Author(s):  
A. M. Hood
Keyword(s):  
Sodium Chloride ◽  
Yeast Extract ◽  
Sodium Phosphate ◽  
Culture Medium ◽  
Culture Media ◽  
Casein Hydrolysate ◽  
Chloride Ion ◽  
Sodium Sulphate ◽  
Hydrolysed Casein

The infectivity ofPasteurella tularensisclouds decreases with age, for guineapigs challenged by the peritoneal and respiratory routes. No decrease occurs in mice challenged peritoneally. The loss of infectivity depends to some extent on age of culture but more especially on culture medium used. Cultures grown in a partially hydrolysed casein medium and aged 2–3 weeks lose infectivity severely in clouds held 20 hr. at 85%r.h., whereas if grown in cysteine broth with catalase (CBC) no loss occurs in this time until cultures are aged several months. Chloride ion, yeast extract and casein hydrolysate are shown to be infectivity depressors when used in culture media or when added to suspensions before spraying. Sodium chloride in CBC can be replaced adequately by sodium sulphate or sodium phosphate for growth of the organism.

Accelerated cheese ripening with heat treated cells of Lactobacillus helveticus and a commercial proteolytic enzyme

1988 ◽  
Vol 55 (2) ◽  
pp. 239-245 ◽  
Author(s):  
Ylva Ardö ◽  
Hans-Erik Pettersson
Keyword(s):  
Proteolytic Enzyme ◽  
Bitter Taste ◽  
Proteolytic Enzymes ◽  
Lactobacillus Helveticus ◽  
Cheese Ripening ◽  
Heat Treated ◽  
Hydrolysed Casein ◽  
Hydrolysis Of ◽  
Microbial Sources ◽  
Hard Cheese

SummarySynergic effects of proteolytic enzymes from two different microbial sources on the ripening of Swedish hard cheese were studied. When extracellular proteolytic enzymes from Bacillus subtilis (Neutrase) and/or heat treated cells of Lactobacillus helveticus (now L. delbrueckii subsp. helveticus) were added to the cheese milk, cheese ripening was accelerated; Neutrase effectively hydrolysed casein to give a softer body. Addition of heat treated lactobacilli did not accelerate hydrolysis of casein, but accelerated the breakdown of peptides which increased the amount of amino acid N in the cheese and also enhanced the intensity of cheese flavour. A bitter taste which developed in cheeses with added Neutrase could be eliminated by the simultaneous addition of heat treated lactobacilli.

scholarly journals Ileal digestibility of dietary protein in the growing pig and adult human

2009 ◽  
Vol 102 (12) ◽  
pp. 1752-1759 ◽  
Author(s):  
Amélie Deglaire ◽  
Cécile Bos ◽  
Daniel Tomé ◽  
Paul J. Moughan
Keyword(s):  
Body Weight ◽  
Dietary Protein ◽  
Human Subjects ◽  
Protein Digestibility ◽  
Sole Source ◽  
Growing Pigs ◽  
Ileal Digestibility ◽  
Adult Human ◽  
Growing Pig ◽  
Hydrolysed Casein

The suitability of the pig as an animal model for predicting protein digestibility in man was evaluated. Healthy adult human subjects (mean body weight 67 kg;n11) and growing pigs (mean body weight 40 kg;n15) were fed semi-synthetic mixed meals containing, as a sole source of N, casein (C), hydrolysed casein (HC) or rapeseed isolate (R). There was no prior adaptation to the test meal. Ileal digesta were sampled through a naso-ileal tube (human subjects) or a post-valve T-caecum cannula (pigs) after ingestion of a bolus meal. The protein sources were15N-labelled. Amino acid (AA) digestibilities were not determined for R. Ileal apparent N digestibility was markedly lower (14–16 %;P < 0·001) in human subjects than in pigs (C, HC, R). Similarly, most apparent ileal AA digestibilities were lower (8 % on average;P < 0·05) in human subjects (C, HC). Ileal true N digestibility was slightly lower (3–5 %;P < 0·001) in human subjects than in pigs (C, HC, R) and most true ileal AA digestibilities were similar (P>0·05) between the species (C, HC). Exceptions were for phenylalanine, tyrosine, lysine, histidine and aspartic acid for which digestibilities were lower (3 % on average;P < 0·001) in human subjects. A similar ranking of the diets was observed for true ileal N digestibility between species. The inter-species correlation for true ileal digestibility was high for N (r0·98 over 3 × 2 data;P = 0·11) and AA (r0·87 over 26 × 2 data;P < 0·0001). Overall, this supports the use of the pig as a model for predicting differences among dietary protein digestibility, especially regarding true ileal N digestibility, in man.

scholarly journals Chitinophaga solisilvae sp. nov., isolated from forest soil

2020 ◽  
Vol 70 (8) ◽  
pp. 4808-4815 ◽  
Author(s):  
Weiwei Ping ◽  
Ying Zhang ◽  
Huancheng Pang ◽  
Jun Zhang ◽  
Dai Li ◽  
...  
Keyword(s):  
Forest Soil ◽  
Type Species ◽  
Genomic Sequence ◽  
Tween 80 ◽  
Rrna Gene ◽  
Strictly Aerobic ◽  
Respiratory Quinone ◽  
Content Type ◽  
Link Type ◽  
Hydrolysed Casein

A Gram-stain-negative, strictly aerobic, non-motile and rod-shaped bacterial strain, O9T, was isolated from a forest soil sample collected at Dai, Xishuangbanna, Yunnan Province, PR China. Strain O9T grew optimally at pH 7.0, at 28‒30 °C and in the absence of NaCl. 16S rRNA gene sequence analysis placed strain O9T within the genus Chitinophaga of the family Chitinophagaceae, with Chitinophaga terrae KP01T (97.8 %), Chitinophaga jiangningensis JN53T (97.7 %), Chitinophaga niastensis JS16-4T (97.4 %), Chitinophaga qingshengii JN246T (97.3 %) and Chitinophaga dinghuensis DHOC24T (97.3 %) as its closest relatives. Strain O9T hydrolysed casein, gelatin and Tween 80. It could not assimilate l-arabinose, l-rhamnose, sucrose, melibiose, gentiobiose or d-fructose as a carbon source. It was negative for esterase lipase (C8) and β-glucosidase. Phosphatidylethanolamine was the predominant polar lipid. The major respiratory quinone of strain O9T was MK-7. Its major fatty acids were iso-C15:0 (34.2 %), C16:1 ω5c (20.9 %) and iso-C17:0 3-OH (12.6 %). The genomic DNA G+C content of strain O9T was 49.0 mol% based on total genome calculations. The average nucleotide identity score between the genomic sequence of strain O9T and that of Chitinophaga terrae KP01T was 72.9%. The Genome-to-Genome Distance Calculator showed that DNA‒DNA hybridization values for strain O9T and Chitinophaga terrae KP01T were 13.6, 21.1 and 14.4%, respectively. Based on the polyphasic taxonomic data, strain O9T represents a novel species of the genus Chitinophaga , for which the name Chitinophaga solisilvae sp. nov. is proposed. The type strain is O9T (=CGMCC 1.12462T=KCTC 32404T).

Sign in / Sign up

Export Citation Format

Share Document