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Three energy‐rich protein (ERP) bars were prepared to meet the daily recommended dietary allowance (RDA) for the protein of Pakistani athletes. The bars were developed using dates, cheddar cheese (CC), whey protein isolate (WPI), roasted chickpea flour, and rice flour in different proportions. Bar #1 contained 64 g dates, 16 g dried apricots, 12 g WPI, and 8 g ripened CC. Bar #2 contained the same proportion of these ingredients with an addition of 12.5 g roasted chickpea flour, while bar #3 contained 6.25 g roasted rice and 6.25 g roasted chickpea flour. All the ingredients were homogeneously mixed into paste to form bars weighing 100–110 g per serving size. These bars were studied for the compositional analysis (moisture, protein, and lipid content), protein characterization through sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE), and in vitro determination of the angiotensin I‐converting enzyme (ACE‐I) antihypertensive activity. Moisture and lipid content in bars were 22% and 0.057%–0.313%, respectively, while protein, fiber, and ash contents varied from 22.3% to 23.6%, 6.66 to 5.81, and 2.12% to 2.44%, respectively. The minimum energy content was recorded (272.70 Kcal/100 g) in bar #1 while bar #3 showed the highest energy content 274.65 Kcal/110 g with the addition of (5%) roasted chickpea and rice flour, respectively. Electrophoresis analysis of proteins in bar # 1 (cheese +WPI) showed the four bands at 62, 24, 20, and 12 kDa. Bar #2 (10% roasted chickpea flour) showed some additional bands at 40, 36, 34, and 28 kDa while relatively lower antihypertensive activity than bars #1 and 3. The study revealed that adding 10% roasted chickpea flour (bar #2) increased the protein content and diversity in proteins. It provided 40% proteins to athletes and could be helpful to meet their R.D.A. by consuming two bars/day. [ABSTRACT FROM AUTHOR]

Ribonucleases belonging to the RNase T2 family are enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryotes. Studies in plants and vertebrates suggest they have an important housekeeping function in rRNA recycling. However, little is known about this family of enzymes in protostomes. We characterized RNase X25, the only RNase T2 enzyme in Drosophila melanogaster. We found that RNase X25 is the major contributor of ribonuclease activity in flies as detected by in gel assays, and has an acidic pH preference. Gene expression analyses showed that the RNase X25 transcript is present in all adult tissues and developmental stages. RNase X25 expression is elevated in response to nutritional stresses; consistent with the hypothesis that this enzyme has a housekeeping role in recycling RNA. A correlation between induction of RNase X25 expression and autophagy was observed. Moreover, induction of gene expression was triggered by oxidative stress suggesting that RNase X25 may have additional roles in stress responses. Phylogenetic analyses of this family in protostomes showed that RNase T2 genes have undergone duplication events followed by divergence in several phyla, including the loss of catalytic residues, and suggest that RNase T2 proteins have acquired novel functions. Among those, it is likely that a role in host immunosuppression evolved independently in several groups, including parasitic Platyhelminthes and parasitoid wasps. The presence of only one RNase T2 gene in the D. melanogaster genome, without any other evident secretory RNase activity detected, makes this organism an ideal system to study the cellular functions of RNase T2 proteins associated with RNA recycling and maintenance of cellular homeostasis. On the other hand, the discovery of gene duplications in several protostome genomes also presents interesting new avenues to study additional biological functions of this ancient family of proteins. [ABSTRACT FROM AUTHOR]

Ribonucleases belonging to the RNase T2 family are enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryotes. Studies in plants and vertebrates suggest they have an important housekeeping function in rRNA recycling. However, little is known about this family of enzymes in protostomes. We characterized RNase X25, the only RNase T2 enzyme in Drosophila melanogaster. We found that RNase X25 is the major contributor of ribonuclease activity in flies as detected by in gel assays, and has an acidic pH preference. Gene expression analyses showed that the RNase X25 transcript is present in all adult tissues and developmental stages. RNase X25 expression is elevated in response to nutritional stresses; consistent with the hypothesis that this enzyme has a housekeeping role in recycling RNA. A correlation between induction of RNase X25 expression and autophagy was observed. Moreover, induction of gene expression was triggered by oxidative stress suggesting that RNase X25 may have additional roles in stress responses. Phylogenetic analyses of this family in protostomes showed that RNase T2 genes have undergone duplication events followed by divergence in several phyla, including the loss of catalytic residues, and suggest that RNase T2 proteins have acquired novel functions. Among those, it is likely that a role in host immunosuppression evolved independently in several groups, including parasitic Platyhelminthes and parasitoid wasps. The presence of only one RNase T2 gene in the D. melanogaster genome, without any other evident secretory RNase activity detected, makes this organism an ideal system to study the cellular functions of RNase T2 proteins associated with RNA recycling and maintenance of cellular homeostasis. On the other hand, the discovery of gene duplications in several protostome genomes also presents interesting new avenues to study additional biological functions of this ancient family of proteins.