Utilization of fermented animal by-product blend as fishmeal replacer in the diet of Labeo rohita

Experiments were carried out to evaluate efficiency of Labeo rohita to utilize fermented animal protein blend containing slaughter house blood (SHB) and fish offal (FO) as dietary fishmeal (FM) replacer. Five isoproteic (30%), isolipidic (8%) and isoenergitic (15.00 kJ g−1) feed were prepared by replacing 0 (T1), 25 (T2), 50 (T3), 75 (T4) and 100% (T5) FM protein with the fermented blend and fingerlings of L. rohita (mean weight 2.07 g) were fed each of these feed in triplicate groups. The results showed that apparent digestibility coefficient (ADC) of protein significantly increased in T3–T5, while ADC of lipid and total amino acid absorption rate increased in T2–T5 as compared to control (T1). Among the essential amino acids (EAA), arginine exhibited maximum absorption followed by histidine, phenylalanine, valine and lysine while aspartic acid showed a high absorption among the non-essential amino acids (NAA). Fish fed up to 75% of replacement level (T4) did not show any significant difference (P < 0.05) in weight gain (WG), specific growth rate (SGR), feed conversion ratio (FCR), protein efficiency ratio (PER) and apparent net protein utilization (ANPU) between the dietary groups (T1–T4). But FCR was increased and other growth parameters were significantly reduced in 100% replacement group (T5), while body muscle protein was significantly reduced in both T4 and T5. Deposition of EAA (except histidine and methionine) in T4 and NAA (except cystine) in both T4 and T5 in the muscle of fish were also significantly reduced as compared to control (T1). Multi-objective optimization programming technique was used to determine FM replacement level that optimized all the growth parameters (WG, SGR, FCR and PER) simultaneously. By using Global Criterion method, it was obtained that 21.11% replacement of FM by the fermented blend was ideal for optimum growth of L. rohita

Autophosphorylation of gatekeeper tyrosine by symbiosis receptor kinase

AbstractPlant receptor-like kinases (RLKs) share their evolutionary origin with animal interleukin-1 receptor-associated kinase (IRAK)/Pelle family of soluble kinases and are distinguished by having tyrosine as ‘gatekeeper’. This position is adjacent to the hinge region and is hidden in a hydrophobic pocket of the catalytic cleft of protein kinases and is therefore least probable to be a target for any modification. This communication illustrates the accessibility of the gatekeeper site (Y670) towards both autophosphorylation and dephosphorylation in the recombinant cytoplasmic domain of symbiosis receptor kinase from Arachis hypogaea (AhSYMRK). Autophosphorylation on gatekeeper tyrosine was detected prior to extraction but never under in vitro conditions. We hypothesize gatekeeper phosphorylation to be associated with synthesis/maturation of AhSYMRK and this phenomenon may be prevalent among RLKs