Protein Nutritive Quality of Commercial Fish Meals as Assessed by Biological and Chemical Methods

1966 ◽  
Vol 23 (3) ◽  
pp. 395-414 ◽  
Author(s):  
B. E. March ◽  
Jacob Biely ◽  
C. Goudie ◽  
H. L. A. Tarr

Various chemical characteristics of fish meals pertaining to the protein and lipid components were determined and their relation to different biological estimates of protein quality were studied. The results demonstrated the practical importance of selecting appropriate biological assays in order to avoid underestimating or overestimating protein quality. Pepsin digestibility of the crude protein remaining in the meals after chloroform–methanol extraction was significantly correlated with biological estimates of protein quality. Meals of initially high supplementary protein value declined in value to a greater extent than did meals of lower quality. The level of available lysine present in the meals declined with storage but biological tests indicated that a combination of several amino acids rather than any single amino acid was limiting to supplementary protein value.

1978 ◽  
Vol 5 (1) ◽  
pp. 19-22 ◽  
Author(s):  
Josephine Miller ◽  
R. Dixon Phillips ◽  
C. T. Young

Abstract Peanut protein supported rapid growth in weanling rats when present in the diet in sufficient quantity. Defatted meal was prepared by cold pressing and hexane extraction of oil from seeds of Florunner, Tifrun, UF 70115, Tennessee Red, Tamnut and Comet cultivars of peanuts. A concentration of 16% peanut protein resulted in better growth than 12% protein from all cultivars tested. Increasing protein to 20% of the diet further improved growth of rats fed meal from some, but not all, cultivars of peanuts. Apparent digestibility of nitrogen in the meals was about 92%. Peanut meal is potentially a good source of protein for animal production if the peanuts and meal are properly handled after harvest to maintain the nutritional quality of the product. Some statistically significant differences occurred in growth performance of rats fed meals from the several cultivars of peanuts but these are not likely to be of practical importance. However, they suggest that protein quality of the peanut might be improved by breeding. The nutritional quality of peanut protein is considered to be low because the concentration of several of the essential amino acids is below optimal levels for promoting growth of young animals. When compared with casein in the accepted bioassay for protein efficiency ratio (PER, Neucere et al., 1972) or by the slope-ratio technique (Hegsted et al., 19680), the biological value is commonly found to be 50 to 75% of that of the standard protein. Such tests are conducted with growth-limiting levels of dietary protein and provide little information on the potential capacity of a protein to support an acceptable rate of growth. Carpenter and de Muelenaere (1965) concluded that, under certain conditions, higher levels of poor-quality proteins would result in nearly as good growth of chicks, pigs, and rats as could be obtained with practical diets containing good-quality proteins. Defatted meal from Florunner peanuts, when incorporated into diets to provide 16.7% protein, supported growth of weanling rats at a rate comparable to that obtained with diets containing 12% to 24% of casein (Miller and Young, 1977). This paper describes results of a study similar to that mentioned above using meal from several cultivars of peanuts that are of current commercial or genetic interest.


Nahrung/Food ◽  
1974 ◽  
Vol 18 (3) ◽  
pp. 243-249 ◽  
Author(s):  
S. G. Kharatyan ◽  
M. G. Kerimova ◽  
A. D. Ignatyev ◽  
M. E. Rozhansky

1980 ◽  
Vol 60 (2) ◽  
pp. 473-480 ◽  
Author(s):  
Y. K. GOH ◽  
D. R. CLANDININ ◽  
A. R. ROBBLEE

Fourteen commercial rapeseed meals (RSM), selected from a total of 63 samples received from six rapeseed processing plants, and one sample of soybean meal (SBM) were tested for protein quality in a chick growth trial. The RSM studied consisted of six pairs, of which each pair of meals represented the meals with the highest and lowest protein solubilities in 0.2% KOH solution among samples received from each plant and one pair of RSM selected in a similar manner from among a second set of RSM samples supplied by one of the processing plants. The protein solubilities of the RSM used in the growth trial ranged from 33.9 to 72.6%. However, the protein quality of the same meals determined biologically by the total protein efficiency (TPE) method were not significantly different (P < 0.05). The TPE values of the RSM varied from 2.57 to 2.71 and were not significantly different from that of soybeam meal (2.65). These results indicate that determination of protein solubility of RSM in 0.2% KOH solution is not a suitable laboratory method of predicting the protein quality of commercial RSM. Other analyses performed on the RSM samples included determination of basic amino acid composition, available lysine content and dye-binding capacity of protein (DBCP) with Acid Orange 12. Of these analyses, only the DBCP values of the meals were found to be significant (P < 0.05) correlated with the TPE values.


1957 ◽  
Vol 37 (1) ◽  
pp. 58-63 ◽  
Author(s):  
T. M. MacIntyre

Studies were made of the variation in quality of commercial fish meals produced in the Atlantic Provinces of Canada. A chick growth method was used for estimating the protein quality of the fish meals. Forty different samples of fish meal were tested. Results indicate that there is considerable variation in the growth-promoting qualities of commercial fish meals. This variation in growth appears to be due to variation in the protein quality of the fish meals.


1980 ◽  
Vol 94 (1) ◽  
pp. 111-116 ◽  
Author(s):  
S. S. Zombade ◽  
G. N. Lodhi ◽  
J. S. Ichhponani

SummaryThe present study was made to evaluate the protein quality of 11 samples of fish meal (FM) covering a wide range of nutrient content to find a suitable laboratory method for predicting nutritive quality. The nutrient content of the samples ranged from 34 to 62% in crude protein, 28 to 48% in true protein and 0·99 to 2·87% in available lysine. The true protein content of FM was further partitioned into myogen, myosin and stroma proteins. The stroma protein accounted for 61% of total crude protein suggesting that a large portion of FM comprised scales, viscera, cartilage, bones and other inedible parts of fish (head, tail, etc.). Neither true protein nor its different fractions was found suitable to detect differences in protein quality of FM although there was an inverse relationship between stroma protein and nitrogen solubility.Available lysine content and relative nutritive value (RNV) were found accurate and reliable laboratory tests for assessing the protein quality of FM. The linear equations to predict gross protein value (GPV) from available lysine content and RNV areGPV = 11·2×% available lysine+34·5;GPV = 0·55×RNV+51.The correlation coefficients between biologically assayed and predicted GPV from available lysine and RNV were 0·71 and 0·62, respectively. The findings suggest that the screening of FM samples for their nutrient content is essential before compounding diets for different categories of chickens.


1974 ◽  
Vol 32 (3) ◽  
pp. 647-660 ◽  
Author(s):  
K. J. Carpenter ◽  
A. A. Woodham

1. Twelve commercial samples of high-protein feeding-stuffs, six of them fish meals, were used for a study of the reproducibility of chemical, microbiological and biological assay values for individual amino acids. Comparisons were also made of results obtained by different methods for the same amino acid.2. For lysine there was quite good agreement between the results from the different laboratory tests for ‘available’ lysine. The values for ‘total’ lysine were, on average, 10 % higher than those for ‘available’ lysine.3. For methionine the correlations between the chick assay and each of the laboratory tests were similar.4. The results from the ‘total protein efficiency’ test of over-all protein quality, using chicks, showed a close correlation with the results of lysine or methionine assays according to which of the two amino acids was most deficient.5. The results with tryptophan were difficult to interpret and no recommendations could be made as to procedures suitable for general use.6. Although most of the present samples proved to be of good quality, only screening of a much larger number of samples will reveal to what extent commercial protein concentrates of low availability are still liable to come onto the market.


1965 ◽  
Vol 22 (1) ◽  
pp. 13-16 ◽  
Author(s):  
I. C. Munro ◽  
A. B. Morrison

Salting and smoking had no effect on the biological value of cod protein, as indicated by Protein Efficiency Ratio, gross protein values, total lysine and methionine content, "available lysine" values, and plasma free lysine and methionine levels in human subjects. It was concluded that smoked and salted codfish can provide protein of high nutritional value.


Molecules ◽  
2021 ◽  
Vol 26 (1) ◽  
pp. 234
Author(s):  
Fatemah B. Alsalman ◽  
Hosahalli S. Ramaswamy

Chickpea cooking water (CCW), known as aquafaba, has potential as a replacement for egg whites due to its emulsion and foaming properties which come from the proteins and starch that leach out from chickpeas into the cooking water. High pressure (HP) processing has the ability to modify the functional characteristics of proteins. It is hypothesized that HP processing could favorably affect the functional properties of CCW proteins by influencing their structure. The objective of this study to evaluate the effect of HP treatment on the associated secondary structure, emulsion properties and thermal characteristics of CCW proteins. A central composite rotatable design is used with pressure level (227–573 MPa) and treatment time (6–24 min) as HP variables, and concentration of freeze dried CCW aquafaba powder (11–29%) as product variable, and compared to untreated CCW powder. HP improves aquafaba emulsion properties compared to control sample. HP reduces protein aggregates by 33.3%, while β-sheets decreases by 4.2–87.6% in which both correlated to increasing protein digestibility. α-helices drops by 50%. It affects the intensity of some HP treated samples, but not the trend of bands in most of them. HP treatment decreases Td and enthalpy because of increasing the degree of denaturation.


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