Environmental Impacts of Large-Scale Spirulina (Arthrospira platensis) Production in Hellisheidi Geothermal Park Iceland: Life Cycle Assessment.

Spirulina algae (Spirulina platensis) cultivated in geothermally powered photobioreactors is here proposed as a potentially resource efficient, zero-carbon, and nutritious alternative to conventional beef meat. Employing a standard life cycle assessment, environmental impacts of large-scale Spirulina production in this facility are calculated. The production facility is sited in Orka náttúrunnar (ON Power) Geothermal Park, Iceland, and benefits from resource streams accessible through Hellisheiði (Hellisheidi) power station, including renewable electricity for illumination and power usage, hot and cold water streams for thermal management, freshwater for cultivation, and CO2 for biofixation. During cultivation, GHG-intensive ammonia-based fertilizers are replaced with macronutrients sourced from natural open mines. LCA results show that production of 1 kg of wet edible biomass in this facility requires 0.0378 m2 non-arable land, 8.36 m3 fresh water and is carbon neutral with - 0.008 CO2-eq GHG emissions (net zero). Compared with conventionally produced meat from beef cattle, Spirulina algae cultured in the ON Power Geothermal Park, referred to in this study as GeoSpirulina, requires less than 1% land and water and emits less than 1% GHGs. Considering food and nutritional security concerns, cultivation in a controlled environment agriculture system assures consistent nutritional profile year-round. Moreover, GeoSpirulina biomass assessed in this study contains all essential amino acids as well as essential vitamins and minerals. While keeping a balanced nutrition, for every kg beef meat replaced with one kg GeoSpirulina, the average consumer can save ~ 100 kg CO2-eq GHGs. It is concluded that environmental impacts of GeoSpirulina production in the Hellisheidi facility are considerably lower than those of conventionally produced ruminants.

Antioxidant supplementation can reduce the survival costs of excess amino acid intake in honeybees.

Over-consuming amino acids is associated with reduced survival in many species, including honeybees. The mechanisms responsible for this are unclear but one possibility is that excessive intake of amino acids increases oxidative damage. If this is the case, antioxidant supplementation may help reduce the survival costs of high amino acid intake. We tested this hypothesis in African honeybees (Apis mellifera scutellata) using the major antioxidant in green tea, epigallocatechin-3-gallate (EGCG). We first determined the dose-range of EGCG that improved survival of caged honeybees fed sucrose solution. We then provided bees with eight diets that differed in their ratio of essential amino acids (EAA) to carbohydrate (C) (0:1, 1:250, 1:100, 1:75, 1:50, 1:25, 1:10, 1:5 EAA:C) and also in their EGCG dose (0.0 or 0.4 mM). We found that bees fed sucrose only solution survived better than bees fed EAA diets. Despite this, bees preferred a diet that contained intermediate ratios of EAA:C (ca. 1:25), which may represent the high demands for nitrogen of developing nurse bees. EGCG supplementation improved honeybee survival but only at an intermediate dose (0.3-0.5 mM) and in bees fed low EAA diets (1:250, 1:100 EAA:C). That EGCG counteracted the lifespan reducing effects of eating low EAA diets suggests that oxidative damage may be involved in the association between EAAs and lifespan in honeybees. However, that EGCG had no effect on survival in bees fed high EAA diets suggests that there are other physiological costs of over-consuming EAAs in honeybees.

Amino acid scoring patterns for protein quality assessment.

The 1985 FAO/WHO/UNU protein report defined reference amino acid patterns for infants based on breast milk and for preschool children, schoolchildren and adults from age specific estimates of dietary indispensible amino acid requirements divided by the safe protein requirement for each age group. This report argued that the protein quality of a diet should be estimated from its digestibility adjusted by its amino acid score calculated from its limiting amino acid in comparison with the reference amino acid pattern. Subsequently a joint FAO/WHO expert consultation on protein quality evaluation (1991) endorsed this protein digestibility-corrected score approach. However it rejected the adult scoring pattern identified in the 1985 report arguing that the amino acid values for this pattern were too low. As an interim measure it suggested that the scoring pattern for preschool children should be used for all age groups apart from infants. The recent WHO/FAO/UNU (2007) report endorsed the 1985 report in recommending the amino acid content of breast milk as the best estimate of infant amino acid requirements. However it was only able to identify reliable requirement values for adults and adopted a factorial approach to derivation of age-related scoring patterns. This utilized the adult pattern for maintenance, and the pattern of human tissue protein for growth. Thus scoring patterns were derived for children aged 0·5, 1-2, 3-10, 11-14, 15-18 years and for adults. The total dietary amino acid requirements calculated for these age groups were divided by the mean protein requirement to give the scoring pattern which should be used to adjust digestible intakes to identify the available protein in specific diets. However because the adult values were determined in subjects at protein intakes much higher than the mean minimum protein requirement, i.e. at 1 g/kg/d rather than 0·66 g/kg/d, the pattern is likely to include higher values than the minimum requirement and should therefore be referenced against the safe allowance.

Assessment of protein adequacy in developing countries: quality matters.

Dietary protein and amino acid requirement recommendations for normal "healthy" children and adults have varied considerably with 2007 FAO/WHO protein requirement estimates for children lower, but dietary essential AA requirements for adults more than doubled. Requirement estimates as presented do not account for common living conditions, which are prevalent in developing countries such as energy deficit, infection burden and added functional demands for protein and AAs. This study examined the effect of adjusting total dietary protein for quality and digestibility (PDCAAS) and of correcting current protein and AA requirements for the effect of infection and a mild energy deficit to estimate utilizable protein (total protein corrected for biological value and digestibility) and the risk/prevalence of protein inadequacy. The relationship between utilizable protein/prevalence of protein inadequacy and stunting across regions and countries was examined. Data sources (n = 116 countries) included FAO FBS (food supply), UNICEF (stunting prevalence), UNDP (GDP) and UNSTATS (IMR) and USDA nutrient tables. Statistical analyses included Pearson correlations, paired-sample/non-parametric t-tests and linear regression. Statistically significant differences were observed in risk/prevalence estimates of protein inadequacy using total protein and the current protein requirements versus utilizable protein and the adjusted protein requirements for all regions (p < 0·05). Total protein, utilizable protein, GDP per capita and total energy were each highly correlated with the prevalence of stunting. Energy, protein and utilizable protein availability were independently and negatively associated with stunting (p < 0·001), explaining 41 %, 34 % and 40 % of variation respectively. Controlling for energy, total protein was not a statistically significant factor but utilizable protein remained significant explaining~45 % of the variance (p = 0·017). Dietary utilizable protein provides a better index of population impact of risk/prevalence of protein inadequacy than crude protein intake. We conclude that the increased demand for protein due to infections and mild to moderate energy deficits, should be appropriately considered in assessing needs of populations where those conditions still prevail.

Protein quality assessment: impact of expanding understanding of protein and amino acid needs for optimal health.

Protein quality describes characteristics of a protein in relation to its ability to achieve defined metabolic actions. Traditionally, this has been discussed solely in the context of a protein's ability to provide specific patterns of amino acids to satisfy the demands for synthesis of protein as measured by animal growth or, in humans, nitrogen balance. As understanding of protein's actions expands beyond its role in maintaining body protein mass, the concept of protein quality must expand to incorporate these newly emerging actions of protein into the protein quality concept. New research reveals increasingly complex roles for protein and amino acids in regulation of body composition and bone health, gastrointestinal function and bacterial flora, glucose homeostasis, cell signaling, and satiety. The evidence available to date suggests that quality is important not only at the minimum Recommended Dietary Allowance level but also at higher intakes. Currently accepted methods for measuring protein quality do not consider the diverse roles of indispensable amino acids beyond the first limiting amino acid for growth or nitrogen balance. As research continues to evolve in assessing protein's role in optimal health at higher intakes, there is also need to continue to explore implications for protein quality assessment.

[Assessment of protein quality in foods by calculating the amino acids score corrected by digestibility]. / Evaluación de la calidad de las proteínas en los alimentos calculando el escore de aminoácidos corregido por digestibilidad.

The protein score reflects its amino acids (AA) content in comparison with the ideal protein. However, when there is a need to know the use of AA by the organism it is necessary to do a correction of the score value by protein digestibility (PDCAAS). Since this information is not available for usually consumed foods, the present work aimed at calculating the PDCAAS values of these foods. The score was calculated the limiting AA of 70 foods, taking as reference protein the AA pattern for children > 1 year old and adults proposed by the U.S. National Academy of Sciences for the year 2002. The PDCAAS value was obtained in each case by multiplying the score value by the digestibility index. For vegetable foods the obtained score values and PDCAAS were, respectively: vegetables 88.5% / 73.4%, tubercles 89.44% / 74.24%, fresh fruits 75.6% / 64.3%, dried fruits 65.6% / 48.1%, legumes in general 89.2% / 69.58%, chickpea and soybean 100% / 78%, cereals and derivatives 68.8% / 58.5%. Creation of table that contents the score values, digestibility values, and PDCAAS of foods is a useful tool when food selection for a dietary plan based on its protein quality is desirable.

Assessment of postruminal amino acid digestibility of roasted and extruded whole soybeans with the precision-fed rooster assay.

The objectives of these studies were to predict the effects of roasting and extrusion temperatures of whole soybeans (SB) on intestinal protein digestibility in cattle. Intestinal digestibility was assessed with a two-stage in vitro or in situ ruminal incubation/precision-fed cecectomized rooster bioassay. In Exp. 1, whole SB (raw SB or SB roasted to 141, 149, or 157 degrees C exit temperature from a commercial roaster and steeped for 30 min) were incubated in strained ruminal fluid and McDougall's buffer (50:50) at 39 degrees C for 16 h. In Exp. 2, SB (ground raw SB or SB extruded at 116, 138, or 160 degrees C) were placed in polyester bags (20 x 30 cm) and suspended in the ventral rumen of steers for 16 h. Lyophilized residue of the in vitro or in situ incubations and samples of raw SB and most extensively heated SB (roasted SB at 157 degrees C or extruded SB at 160 degrees C) for each respective experiment were crop-intubated to cecectomized roosters. Total excreta were collected for 48 h after intubation and lyophilized, and amino acid (AA) concentrations were determined. In Exp. 1, total AA digestibility was 61.6 and 84.5% for unincubated whole raw SB and 157 degrees C roasted SB, respectively, and 66.2, 88.9, 91.3, and 91.6% for in vitro residues of whole raw SB and SB roasted at 141, 149, and 157 degrees C, respectively. Trypsin inhibitor (TI) activity was 20.09, 1.69, 1.54, and 1.84 mg/g fat-free DM for unincubated whole raw SB and 141, 149, and 157 degrees C roasted SB, respectively, and 30.84, 1.01, .90, and .26 mg/g fat-free DM for in vitro residues of whole raw SB, 141, 149, and 157 degrees C roasted SB, respectively. In Exp. 2, total AA digestibility was 68.5 and 87.7% for unincubated ground raw SB and 160 degrees C extruded SB, respectively, and 81.9, 91.3, 89.7, and 89.4% for in situ residues of ground raw SB and 116, 138, and 160 degrees C extruded SB, respectively. Trypsin inhibitor activity was 17.61, 4.89, 4.08, and 1.56 mg/g fat-free DM for unincubated ground raw SB, 116, 138, and 160 degrees C extruded SB, respectively, and 3.62, .59, .55, and .21 mg/g fat-free DM for incubated ground raw SB, 116, 138, and 160 degrees C extruded SB, respectively. Heat treatment by roasting and extrusion improved AA digestibilities of SB, but there were no differences detected among the roasting or extrusion temperatures. Ruminal fermentation did not eliminate the negative effects of TI activity on intestinal digestibility of AA in whole SB but did reduce TI activity in ground SB.

Post-prandial plasma aminograms in the assessment of protein quality for young children: maize and grain amaranth, alone and combined.

Post-prandial (p.p.) changes in plasma free amino acid (AA) concentrations of children consuming a single source of protein at critical levels are determined by its digestibility and total essential AA/total AA ratios; the molar proportion of the limiting EAA (EAA/TEAA), if any, will fall significantly in plasma as it is utilized more completely than others. Grain amaranths (Am), reputedly rich in lysine (Lys) and tryptophan (Trp), but moderately deficient in leucine (Leu), should be ideal complements to Lys and Trp-poor, Leu-rich maize (M). Most animal studies confirm this. In children, 20, 30 and even 50 per cent replacement of M proteins with toasted Am proteins had failed to show any gains over M or Am alone: heat losses of Lys were suspected. Plasma obtained during the above studies, before and 3 h and 4 h after the first meal of the last day of consuming Am alone, three M-toasted Am mixtures, or M alone, were analysed for free AAs. Toasted, popped or flaked Am consumption caused significant p.p. falls in molar proportions of Leu from 99 to 85, 88 to 82, and 92 to 75, and of threonine (Thr) from 118 to 108 (popped) and 109 to 97 (flaked) mmol/mol TEAA, suggesting that these were first- and second-limiting EAAs. Post-prandial fall in Lys proportion was questionably significant. The M diet produced highly significant 3-h Leu elevation from 132 to 187, Lys fall from 167 to 135, and Trp fall from 62 to 46 mmol/mol TEAA.(ABSTRACT TRUNCATED AT 250 WORDS)

Relation between in vitro and in vivo assessment of amino acid availability.

Even though the availability of dietary amino acids is the result of integrated phenomena of digestion, absorption and transport, it may be mainly affected by the stage of luminal digestion. In this case, amino acid availability could be predicted by an in vitro method designed to reproduce in vivo proteolysis conditions. In order to check this hypothesis, the essential amino acid (EAA) profiles of digesta collected at 8 intervals during a 24-h in vitro enzymatic proteolysis of casein and rapeseed proteins were compared to the pattern of appearance of dietary EAA in portal vein of pigs fed the same proteins, determined at each hour over a 8-h postprandial period by coupling blood flow rate with porto-arterial differences in plasma EAA concentrations. Comparisons of in vitro and in vivo data first bore on overall EAA profiles measured at each interval, and then on the individual kinetics of each EAA. Regarding total profiles, the highest correlations for casein (r: 0.80-0.98) were found when comparing EAA patterns determined during the first half of in vitro digestion and in vivo absorption periods. Similar r values were obtained with rapeseed proteins, but over longer periods of measurement. Concerning individual kinetics, the highest correspondences were found with rapeseed proteins, with 5 out of 9 EAA (methionine, isoleucine, leucine, phenylalanine and arginine) having their in vitro sequence of release significantly correlated with their in vivo sequence of absorption. With casein, correlations were significant for threonine, valine, isoleucine and leucine. These results suggest that sequential hydrolysis in the digestive tract, as reproduced by the in vitro technique, is a key determinant of amino acid appearance in the portal blood to a degree varying with the protein source and with the nature of the amino acid.

Protein and amino acids of breast milk from Thai mothers.

The protein, amino acids, and nonprotein nitrogen of milk samples obtained from Thai mothers over a period of 0 to more than 270 days postpartum were determined. Protein levels decreased from 1.56% during the 1st wk to a low of about 0.6% from 180 to 270 days and then rose to about 0.7%. The amino acid pattern of the milks suggested a number of differences in their composition and those of samples analyzed in other countries. Nonprotein nitrogen varied from 20 to 40% of the total nitrogen of the milk. It has been concluded that the need for supplementation of breast-fed Thai babies may occur earlier than many nutritionists advocate.

PIP: This study evaluates the effects of prolonged lactation on the quantity of protein and pattern of amino acids in breast milk of 135 Thai women at various times of lactation (from 0 to 270 days postpartum). Breast milk samples were collected approximately 3 hours after nursing at various times during 1978. Total nitrogen, tryptophan and amino acids were respectively analyzed by the methods of Williams, Lorenzo-Andreu and Frandsen and Matheson, and Hitachi Perkin-Elmer Model KLA3B amino acid analyzer. Protein level in breast milk was highest during the 1st week (1.56%) and decreased steadily with time until a level of 0.60% during the period of 180 to 270 days, after which protein content appeared to increase. Ratio of essential to nonessential amino acids was constant throughout the study. Protein or amino acid levels during lactation were not significantly affected by maternal age and parity, although maternal age, parity and socioeconomic factors had been known to affect total milk secretion. Amino acid levels in this study were generally similar to reported values from American and Scottish women, although methionine, valine and tyrosine were lower and tryptophan and lysine were higher. Although breast milk has a nutritional value of the highest quality, it can be argued that the need for supplemental feeding may still occur earlier in life than is often realized. A discussion of the FAO/WHO standards for protein allowances suggests that infants up to 3 months of age require approximately 2 or more g of milk protein per kg daily, while children 60 to 12 months of age require about 1.5 g/kg/daily. Considering that protein content of Thai breast milk is about 0.9% after 3 months of lactation, it is estimated that 1250 ml of milk are needed to supply the protein needs of a 3-month old child, and 950 ml would be insufficient (average daily production of milk varies from 850 ml to 1200 ml). Many Thai and other women who are exclusively breastfeeding may find it difficult to provide the protein needs of their infants, unless supplemental feeding is carried out.