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L D Satterlee

Publications and source records attributed to L D Satterlee.

10 recordsLinked to original sources
PubMed1987

Induced non-enzymatic browning of soybean meal. I. Effects of factors controlling non-enzymatic browning on in vitro ammonia release.

Non-enzymatic browning was tested as a means of suppressing degradation of soybean meal (SBM) by ruminal microbes in five trials with in vitro ammonia release as the response criterion. Treatments imposed on SBM included reducing sugar source (xylose, glucose, fructose and lactose), reducing sugar level (1, 3 and 5 mol/mol SBM-lysine), pH (6.5, 8.5 and 10.0), dry matter (DM) content (65, 70, 75, 80, 85 and 90%) and varying lengths of heating time (0 to 90 min) at 150 C. Samples heated under conditions that promoted non-enzymatic browning gave greater (P less than .01) ammonia release suppression that when SBM was heated without these treatments. Xylose was the most reactive sugar, but extended heating of SBM containing glucose, fructose or lactose resulted in ammonia release similar to xylose. Increasing sugar level from 1 to 5 mol/mol SBM-lysine caused linear decreases (P less than .01) in ammonia release for xylose, glucose and fructose, but not lactose. Ammonia release was higher (P less than .01) at pH 6.5 than pH 8.5 and 10.0, and higher (P less than .01) at pH 9.5 than pH 10.0. Rate of non-enzymatic browning decreased when samples containing greater than 80% DM were heated. These results are interpreted to show that controlled non-enzymatic browning may be effective for reducing ruminal degradation of SBM.

Amines↗
PubMed1987

Induced non-enzymatic browning of soybean meal. II. Ruminal escape and net portal absorption of soybean protein treated with xylose.

Non-enzymatic browning was tested as a means of increasing ruminal escape of soybean meal N. Soybean meal was treated with xylose (3 mol/mol SBM-lysine), sodium hydroxide (pH 8.5) and enough water to achieve an 83% dry matter mixture and then heated at 150 C for 30 min (XTS-30). Trial 1 evaluated ruminal escape of N from XTS-30 compared with commercial soybean meal (CS) or urea (U) in a replicated 3 X 3 Latin square design using six duodenally cannulated Angus X Hereford steers (24.7 kg). Duodenal flow of dietary N was higher (P less than for steers fed XTS-30 (47.9 g/d) than for steers fed CS (39.5 g/d). The ruminal escape estimate for XTS-30 (33.7%) was higher (P less than .10) than CS (13.1%), whereas total tract apparent N digestibility was not different among treatments. In trial 2, net portal absorption of alpha-amino N was measured in Finnsheep X Suffolk ram lambs (24.7 kg) fed U, CS or XTS-30 in a 3 X 3 Latin square design. Portal blood flow was measured by primed, continuous infusion of para-aminohippuric acid. Portal blood flow was lower (P less than .05) for U.fed lambs than for lambs fed CS or XTS-30, and tended to be lower for lambs fed CS than those fed XTS-30. Net portal absorption of alpha-amino N tended to be lowest for lambs fed U (281 mmol/d) and highest for lambs fed XTS-30 (578 mmol/d). The results are interpreted to show that non-enzymatic browning increased flow of soybean meal N to the intestine.

Animal Feed↗
PubMed1987

Induced non-enzymatic browning of soybean meal. III. Digestibility and efficiency of protein utilization by ruminants of soybean meal treated with xylose or glucose.

Trials were conducted to evaluate effects of non-enzymatic browning of soybean meal (SBM) on efficiency of protein utilization and N digestibility. In trial 1, 48 Suffolk-Finnsheep lambs (22 kg) were fed 80 d to evaluate efficiency of protein utilization for growth when supplemental protein was fed as urea (U), commercial SBM (CS), or commercial SBM (pH 8.5, 83% dry matter) containing xylose (3 mol/mol SBM-lysine) and heated 30 min (XTS-30) or 55 min (XTS-55). Diets containing graded levels of N from CS, XTS-30 and XTS-55 were fed. Response criterion was efficiency of protein utilization, plotted as gains of lambs fed test proteins minus gain of lambs fed U vs supplemental test protein fed. Efficiencies of protein utilization were .62, 1.27 and .91 for CS, XTS-30 and XTS-55, respectively. Protein from XTS-30 was used more efficiently (P less than .05) than that from CS. In trial 2, apparent digestibility of N from CS (97%) was higher (P less than .01) than XTS-30 (77%) and XTS-55 (82%) by Suffolk-Finnsheep lambs (27 kg). In trial 3, 60 mixed-breed steers (218 kg) were fed individually for 105 d to evaluate glucose as a reducing sugar. Glucose-treated SBM (GTS) was prepared by mixing glucose (3 mol/mol SBM lysine) with SBM, adjusting pH and dry matter content to 8.5 and 80%, respectively, and heating at 150 C for 60 min. Supplemental N sources were U, CS, GTS and a 50:50 mixture (protein basis) of corn gluten meal and blood meal (CGM/BM).(ABSTRACT TRUNCATED AT 250 WORDS)

Animal Feed↗
PubMed1982

In vitro assay for predicting protein efficiency ratio as measured by rat bioassay: collaborative study.

Seven laboratories collaborated in testing the calculated protein efficiency ratio (C-PER and DC-PER). The collaborative study required each laboratory to analyze 6 foods and a control protein (ANRC casein) for in vitro apparent protein digestibility, amino acid composition, and PER via rat bioassay. The 6 foods or food ingredients tested were nonfat dry milk, cooked chicken muscle, protein-fortified dry breakfast cereal, textured soy protein, oat-based dry breakfast cereal, and durum wheat flour. Data obtained from the study were analyzed statistically for the intralaboratory variation for each method of analysis (i.e., amino acid analysis, PER, etc.). The ability of the C-PER to rapidly predict rat PER was also measured. The C-PER and DC-PER methods were adopted official first action.

Amino Acids↗
PubMed1980

Protein digestibility of the same protein preparations by human and rat assays and by in vitro enzymic digestion methods.

The apparent and true digestibilities of the same preparations of six proteins (spray dried whole egg, cottage cheese, canned tuna, peanut flour, soy isolate, and wheat gluten) were estimated in four to five men and in rats and compared to estimates of digestibility from three different in vitro enzymic digestion procedures. For all six proteins, the correlation coefficient was 0.46 between true digestibility in humans and in rats; with values for tuna excluded, r = 0.96. With all six proteins, none of the in vitro values was significantly correlated with values from humans or rats. However, with either the three animal proteins alone or the three plant proteins alone, correlations were high (r greater than 0.90) between one or more of the in vitro estimates and the observed true or apparent human and rat digestibilities. The differences in the relationship between enzymic digestion estimates and the human digestibility estimates for plant or animal proteins suggest that for accurate prediction of protein digestibility in humans by these enzymic methods, different equations would have to be used for plant and animal proteins. For protein sources containing both plant and animal protein, use of the in vitro enzymic procedures would give only an approximate estimate of digestibility in humans.

Adult↗
PubMed1969

Effect of meat and isolated meat proteins on the thermal inactivation of staphylococcal enterotoxin B.

The thermal inactivation of staphylococcal enterotoxin B was studied in a phosphate-saline buffer, in the presence of two meat proteins, myosin and metmyoglobin (MetMb), and in a ground-beef slurry. When enterotoxin B was incubated at temperatures from 60 to 110 C, it was shown that the initial thermal inactivation at 80 C was faster than at 100 or 110C. The heating of enterotoxin B at 60, 80, and 100 C in the presence of either myosin or MetMb resulted in a rapid loss of the enterotoxin. Thermal loss of the enterotoxin B molecule in the presence of meat proteins was more pronounced at 80 C than at either 60 or 100 C. Thermal loss of enterotoxin B molecule in the presence of meat proteins was more pronounced at 80 C than at either 60 or 100 C. Thermal loss of enterotoxin B in a ground round slurry was rapid when compared to inactivation in a phosphate-saline buffer. The rapid loss of enterotoxin B in the slurry may be due to a combination of thermal inactivation and the binding of enterotoxin molecules to meat proteins.

Buffers↗
PubMed1969

Response of white mice to cells and culture constituents of Clostridium perfringens.

Broth cultures of Clostridium perfringens (ATCC 10543) were fractionated by ammonium sulfate precipitation and Sephadex G-150 chromatography. Components isolated, as well as some enzymes present in the culture, were assayed for toxicity by feeding to white mice. Early work indicated that when a meat-fat-starch slurry, infected with C. perfringens, was fed to mice, the intestinal passage time was reduced. By using large numbers of mice as test animals and analyzing the data statistically, we found that C. perfringens and several fractions from the culture supernatant significantly affected the mice. A toxic material present in the supernatant was not identifiable as phospholipase C. Phospholipase C and physphorylcholine affected the intestinal passage time of the mice only when large amounts were given. The enzyme, neuraminidase, and another unidentified compound present in the supernatant affected the passage time when very small amounts were fed to mice.

Animal Feed↗