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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<.05) than that from CS. In trial 2, apparent digestibility of N from CS (97%) was higher (P<.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). Efficiencies of protein utilization were .90, 1.91 and 1.85 for CS, GTS and CGM/BM, respectively. Efficiency of protein utilization of GTS was higher (P<.05) than CS but not different (P>.10) from CGM/BM. In trial 4, apparent digestibility of N from CS (100%) was higher (P<.05) than GTS (93%) by Suffolk-Finnsheep lambs (40 kg). These results are interpreted to indicate that controlled, non-enzymatic browning improved efficiency of soybean protein utilization by ruminants.

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 × 3 Latin square design using six duodenally cannulated Angus × Hereford steers (24.7 kg). Duodenal flow of dietary N was higher (P<.01) 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<.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 × Suffolk ram lambs (24.7 kg) fed U, CS or XTS-30 in a 3 × 3 Latin square design. Portal blood flow was measured by primed, continuous infusion of para-aminohippuric acid. Portal blood flow was lower (P<.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.

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<.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<.01) in ammonia release for xylose, glucose and fructose, but not lactose. Ammonia release was higher (P<.01) at pH 6.5 than pH 8.5 and 10.0, and higher (P<.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.

New sources of high quality protein are needed for human consumption. Alfalfa (Medicago sativaL.) is well known for its high yield of protein. Knowledge of genetic variation for protein concentrate yield among cultivars is needed. The alfalfa cultivars ‘Dawson’, ‘Kanza’, ‘Team’, and ‘Weevlchek’ were planted in field plots at the Mead Field Laboratory, Lead, Nebr., in 1972. Forage of the cultivars was harvested and sampled as three growth stages, bud, one‐tenth bloom, and full bloom, in the first and second cuttings of 1973. Forage samples were used for chemical analyses of fresh forage, pressing juice in the laboratory, protein extraction, and subsequent chemical analyses. The purposes of the study were to determine the yield of an alfalfa protein concentrate (without chloroplasts) (APC) from four cultivars at three growth stages, the forage yield and quality of fresh forage, and to determine the recovery and nutrient levels in the residue of processed forage. The cultivars did not differ in dry matter,protein,and carotene levels of fresh forage at any growth stage in either the first or second cutting. The percentage of protein in APC's did not differ among cultivars at any growth stage in either cutting and averaged 76%. Forage and APC yields differed among Cultivars. The lowest forage and APC yields were obtained from Kanza. About 1% of the fresh weight of alfalfa was recovered as APC. APC yield averaged about 200 kg/ha over cultivars and cuttings. APC recovery percentages differed among cultivars and the lowest recovery was from Kanza. Protein recovery decreased as physiologic mauturity increased. At one‐tenth bloom, average protein level of fresh forage was 18.6% compared with 16.4% protein in the residue after pressing (juice extraction), a 12% reduction due to processing. Average carotene level of fresh forage was 190 mg/kg, and carotene level of the residue was 145 mg/kg at one‐tcnth bloom, a 24% reduction. The yield of an alfalfa protein concentrate that contained 76% protein, potentially suitable for human consumption, vaned among cultivars as shown in this preliminary study.

A nondestructive indicator of instantaneous seed growth rate in soybean [Glycine max(L.) Merr.] and other legumes would useful in studies of the physiology of seed growth. The responsiveness of soybean fruit respiration rate to whole plant environmental treatments known to affect photosynthate supply and seed growth was evaluated. Dark respiration (CO2efflux) rates of individual, intact soybean fruits at the mid‐pod‐filling stage were measured while manipulating photosynthetically active radiation (PAR) or ambient CO2concentration in growth chambers. The PAR levels employed were 450, 110, or 30 μmol m−2s−1and CO2concentrations were 300 or 150 μL L−1. Fruit respiration rate.began to decline within 24 h after plants were subjected to either decreased PAR or CO2concentration. After 2 to 3 days the response was complete and fruit respiration rate remained constant at a level determined by the treatment for an additional 4 days, the longest period evaluated. The respiratory response was rapidly reversible when either PAR or CO2concentration were returned to control levels. As PAR was lowered from 450 to 110 or 30 μmol m−2s−1, seed growth rate declined from 20.3 to 11.0 or 8.7 mg day−1fruit−1, respectively. Fruit respiration and seed growth were apparently responding to changes in photosynthate supply. The results indicate that in situ fruit respiration rate is responsive to changes in the physiological status of the plant and may be useful as an indicator of instantaneous seed growth rate in some situations.

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. perfringensand 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.

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.