IN VITRO OBSERVATIONS ON FACTORS AFFECTING CALF PREGASTRIC ESTERASE ACTIVITY

1979 ◽  
Vol 59 (1) ◽  
pp. 1-9 ◽  
Author(s):  
K. J. JENKINS

Three in vitro experiments were conducted to determine the efficacy of calf pregastric esterase (PGE) for hydrolyzing various fats and the influence of various factors on its lipolytic activity. Calf PGE was effective in hydrolyzing butterfat and coconut oil, hydrolyzed smaller amounts of the other plant oils tested and had a very limited capacity for lard and the six grades of tallow studied. The esterase retained good lipolytic activity for butterfat over the pH range normally encountered in the calf abomasum after feeding liquid diets. Rennet clotting of reconstituted skim-milk at pH 6.1 reduced enzyme hydrolysis of butterfat by 30%, presumably due to fat occlusion in the clot. Lecithin, skim-milk powder, casein, and lactalbumin markedly increased PGE activity; Ca++ had no effect. The bile salts taurodeoxycholate, glycochenodeoxycholate and taurochenodeoxycholate markedly inhibited PGE lipolysis, whereas others (taurocholate, deoxycholate, cholate, glycocholate) had little or no effect.

1981 ◽  
Vol 61 (2) ◽  
pp. 393-401 ◽  
Author(s):  
K. J. JENKINS ◽  
J. R. LESSARD ◽  
D. B. EMMONS

The formation of a firm rennet (chymosin) curd in the abomasum appears to have a useful physiological function in the newborn calf. The results of in vitro experiments with calf milk replacers conducted to study the effect of various factors on rennet clot formation demonstrated that low-pressure (L) dispersion of lipid into skim milk powder replacers resulted in markedly higher (P < 0.05) curd firmness values with rennet than homogenization (H) at all total solid (10, 15 and 20%) and lipid (10, 20, 30 and 40% TS) levels tested. At higher total solids levels, curd firmness, clot weight and percentage of replacer lipid in clot were significantly (P < 0.05) increased. The L dispersion method also promoted rennet coagulation and firmer curds than H when skim was partially replaced by mixtures offish protein-whey or Promine D-whey. The results indicate that reconstitution of milk replacers at high total solids levels (e.g., 20%), in conjunction with L dispersion of lipid, would be beneficial for promoting rennet coagulation, curd firmness and high concentrations of protein and lipid in the clot.


1976 ◽  
Vol 56 (2) ◽  
pp. 317-325 ◽  
Author(s):  
D. B. EMMONS ◽  
E. E. LISTER

Fresh milk coagulates with chymosin (rennin) in the calf stomach to form relatively strong curds. With respect to calf milk replacers it is of interest to study factors affecting curd formation of reconstituted skim milk powder by this enzyme. Curd firmness was increased by lower pH of the skim milk over a range of 5.6–6.6, higher concentration of skim milk solids over a range of 5–20%, higher concentrations of chymosin, lower temperatures of heat treatment of skim milk prior to spray drying, and higher temperature of coagulation, 37 vs. 30 C. Reconstitution of powder in water above 56 C for 2 min remarkedly reduced the firmness of the curd. The following coagulation conditions were selected for comparison of powders and milk replacers: addition of 1 ml of a 1:50 dilution of standard strength commercial rennet to 100 ml of milk previously adjusted to pH 6.1, 10% of nonfat solids in the aqueous nonfat phase, temperature of 37 C, and measurements of firmness 30 min after adding rennet. Commercially produced skim milk powders designated high-heat, medium-heat and roller products yielded soft curds. Commercial low-heat powders yielded strong curds. All coagulated in less than 4 min at pH 6.1, the time being relatively independent of heat treatment.


1969 ◽  
Vol 23 (4) ◽  
pp. 763-782 ◽  
Author(s):  
H. Tagari ◽  
J. H. B. Roy

1. Four Ayrshire bull calves between 8 and 34 days of age and fitted with duodenal and ileal re-entrant cannulas were used to study the effect of heat treatment of the milk they received on the pH and nitrogen composition of the pyloric outflow and ileal contents.2. Milk A contained a spray-dried skim-milk powder pre-heated during the drying process at 74° for 30 min and milk B a similar powder pre-heated at 77° for 15 sec. In milk A about 50% of the non-casein protein N had been denatured.3. Milk B resulted in a lower pH than milk A in the pyloric outflow throughout the sampling period of 6.5 h after feeding. It resulted also in an increased volume of outflow during the 1st h after feeding, a reduced output of undigested protein, an increased output of non-protein nitrogen (NPN) and a different pattern of flow of NPN during the first 4 h after feeding.4. These differences between milk A and milk B were associated largely with different clotting characteristics, which were demonstrated in vitro at two levels of addition of rennet with or without the addition of calcium. The buffering capacity of the two milks was similar.5. Variation between calves in their response to these two milks was attributed to the age of the calves and to differences in inherent clotting or proteolytic activity.6. In the ileal outflow, bacterial activity, as measured by dehydrogenase activity, was positively related to N concentration, but the N concentration when milk A was given did not appear to differ from that when milk B was given.7. One calf had diarrhoea when given milk A at a young age. This was associated with an increased pyloric outflow, an increased outflow of undigested protein but little difference in the rate of proteolysis, and a high pH. In the ileal outflow the volume and amount of N was much increased although the N concentration was reduced.8. It is concluded that the detrimental effect of milk A, found in earlier experiments, was largely associated with high pH and poor digestibility of protein in the abomasum, conditions which allow multiplication of coliform organisms in the intestine.


1989 ◽  
Vol 69 (3) ◽  
pp. 727-734 ◽  
Author(s):  
P. S. MIR ◽  
J. H. BURTON ◽  
B. N. WILKIE ◽  
F. R. VAN DE VOORT

The effect of processing commercial soybean meal (HSBM) by either extrusion (ExSBM) or fermentation with microbes in rumen fluid (FSBM) on rate of protein hydrolysis and the activity of the antigen β-conglycinin was evaluated. Ethanol-extracted soybean meal (EtSBM) and skim milk powder (SMP) were included as positive controls while HSBM was the negative control, with regard to antigen content. The rates of proteolysis were determined by acid pepsin hydrolysis and the activity of β-conglycinin in the soluble fraction of the digestion mixtures at 0, 2, 4, 6 and 8 h of in vitro proteolysis was determined by radial immunodiffusion in agar gel containing antibody specific for the antigen. Susceptibility of FSBM and ExSBM to proteolysis by pepsin was greater than that of EtSBM. β-Conglycinin content was greatest in HSBM (1.0 ± 0.2 g dL−1) and only 0.3 ± 0.03 g dL−1 in ExSBM at the beginning of in vitro digestion. The antigen was not detected in either FSBM or EtSBM, therefore these products could be used in milk replacers for calves. Key words: In vitro pepsin proteolysis, extruded soybean meal, fermented soybean meal, antigen, β-conglycinin


1984 ◽  
Vol 51 (4) ◽  
pp. 623-628 ◽  
Author(s):  
Donald Stead

SummaryA method which was developed for assaying the extracellular lipases of psychrotrophic bacteria in milk (Stead, 1983, 1984) and which uses the fluorogenic substrate 4-methylumbelliferyl oleate has been adapted for use with skim milk powder (SMP), whey powder (WP) and whey protein concentrate (WPC). A five-fold increase in the concentration of sodium taurocholate (NaTC), in the mixture of NaTC and cetyltrimethylammonium bromide needed to dissociate lipase from milk proteins, removed the excessive sensitivity of the assay to variations in the concentrations of SMP, WP or WPC incorporated. Commercially available pancreatic lipase provided a suitable standard of lipolytic activity and as little as 1–2 μ could be detected in each assay system.


Data in Brief ◽  
2018 ◽  
Vol 21 ◽  
pp. 911-917 ◽  
Author(s):  
Lotti Egger ◽  
Patrick Schlegel ◽  
Christian Baumann ◽  
Helena Stoffers ◽  
Dominik Guggisberg ◽  
...  

Author(s):  
A. Ruba Nanthini ◽  
C. Valli ◽  
L. Radhakrishnan ◽  
D. Balasubramanyam ◽  
A. Mangalagowri

Background: Rumen fluid has been used as microbial inoculum to treat indigestion in ruminant animals and to conduct in vitro rumen fermentation experiments. Lyophilization of the goat rumen fluid will provide continuous supply of rumen inoculums either for laboratory studies or for transfaunation in treating digestive disorders sequelae to high grain rations. However, no standard protocol is available for lyophilizing goat rumen fluid. Hence, this study was designed to develop a protocol to lyophilize goat rumen fluid as an alternate source for fresh goat rumen fluid. Methods: The study was conducted using 5 × 3 × 3 factorial design with four different cryoprotectants viz., 10% skim milk powder, 10% skim milk powder + 5% sodium glutamate, 5% glycerol, 5% DMSO and no cryoprotectant, at three pre freezing (2, 24 and 48 hours) and three freeze drying (8, 24 and 32 hours) time intervals to standardize protocol for lyophilizing goat rumen fluid. The viability of rumen microbes in the “lyophilized goat ruminal inoculum”, was determined via in vitro gas production study. Result: Pre freezing (-80°C deep freezer) duration of 48 hours with 32 hours of time duration in lyophilizer (-45°C) was ideal for lyophilizing goat rumen fluid with or without the addition of various cryoprotectants. Glycerol used at 5% as cryoprotectant resulted in significantly (P less than 0.05) highest gas production at all (12, 24 and 48) incubation hours studied indicating better viability of rumen microbes.


2016 ◽  
Vol 3 (4) ◽  
Author(s):  
BINITA RANI

The consumers over whelming interest for functional foods, including probiotics have resulted in attempts to develop an indigenously developed food mixture containing pearl millet, chickpea, skim milk powder and tomato pulp (2:1:1:1 w/w). The mixture was autoclaved, cooled and fermented with a probiotic Lactobacillus acidophilus-R at 37o C for 24 h. Both the antinutrients i.e. phytic acid and polyphenols were reduced significantly after autoclaving as well as fermentation whereas in vitro digestibility of starch and protein was significantly (P less than 0.05) improved. A significant negative relationship was obtained between the content of antinutrients and digestibilities.


1982 ◽  
Vol 49 (2) ◽  
pp. 265-278 ◽  
Author(s):  
Gonca Sukan ◽  
Anthony T. Andrews

SUMMARYWith either Na caseinate or skim-milk powder, 1% (w/v) additions of pepsin, chymotrypsin or Alcalase and an incubation time of 24 h at 37°C gave the best hydrolysates for subsequent plastein production. In spite of the fact that peptide species which were produced by treatment with the 3 enzymes were entirely different, they were all capable of producing qualitatively similar amounts of plastein when concentrated and further incubated with proteinase, suggesting that the identity of peptide components was relatively unimportant. αs1-, β- and κ- caseins, Na-caseinate and skim-milk powder all led to plastein products with broadly similar properties, confirming the comparative unimportance of peptide composition. This also indicated that for most practical applications fractionation of initial protein mixtures (as in many food products) would not be justified. Optimum peptide concentration for plastein formation with pepsin and caseinate hydrolysates was 20–35% (w/v) with an optimum pH range of 4–5; the best peptide molecular weight varied between 400 and 800 and the optimum temperature was either 37°C for 24 h or 50°C for 4–6 h. Higher temperatures (70°C) gave more rapid plastein formation but poorer yields. Lower temperatures (e.g. 20°C) gave similar yields, but incubation times required to be extended to at least 48 h. The same proteinase should be used for plastein synthesis as that used in the initial hydrolysis stage, or else further hydrolysis (over hydrolysis) could occur during the plastein formation stage causing lower yields due to differences in the specificity of the 2 enzymes. Even under ideal conditions plastein yields never exceeded 27% of the weight of peptide taken and at the present time it seems unlikely that the plastein reaction will have anything more than curiosity value. Economics must preclude its application in low-cost, high volume situations such as generally exist within the food industry.


Author(s):  
Prakash Goudanavar ◽  
B. Ramesh ◽  
Santosh Fattepur ◽  
Nagaraja Sreeharsha

Objective: The focus of this research has been to improve efficacy, decrease tolerance and increase the irinotecan pharmacokinetic profile. Methods: Proniosomesformulated with various surfactants, cholesterol and dicetyl phosphate using the slurry method. A slurry process was used to prepare proniosomes with maltodextrin as the carrier by using surfactants span 20, span 60, tween 20 and tween 80. Results: The preparations were characterized in terms of shape and specific surface area, entrapment efficacy, in vitro release studies, in vivo tissue diffusion and stability testing. The proniosome surface was found to be smoother in nature showing thin and compact layer with skim milk powder. For formulation 2 (73.94±2.8%), the maximum entrapment efficacy was found. Conclusion: The formulation 3 obtained the desired maximum release profile within 24 hours (98.06%). The in vivo tissue distribution studies for the proniosomes reveal that the drug was preferentially targeted to liver followed by the alveolus and lymphatic system.Stability studies have indicated that the most acceptable condition for storage of the formulation 2 was 4o C. Proniosomes provide an acceptable method to the carrier for targeted therapy. These can be held at specific sites and can release the drug for a prolonged period of time.


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