Peptide hydrolysate (PH) was produced by deep controllable bioconversion of poultry processing leftovers (broiler necks), by means of a multienzyme composition, containing four commercially available enzyme preparations (Alcalase, Neutrase, Flavourzyme, Protamex). The design of multienzyme composition (MEC) was applied to yield a hydrolysate with adjusted properties, including minimized antigenicity and bitterness.The protein recovery was optimized using Box–Behnken response surface design. The individual and interactive effects of hydrolysis conditions (time, hydromodule and MEC dosage) were studied. The experimental data were analyzed by ANOVA method and a well-predictive, second order polynomial model was developed using multiple regression analysis. Optimal hydrolysis conditions were found to be: hydrolysis time 3h, hydromodule 2.25l/kg and dosage of MEC 0.25%. The corresponding predicted value for protein recovery was 75.34%, 2 times higher compared to traditional long-term heating hydrolysis. The PH obtained is a low allergenic product with high antioxidant capacity.

Physical loading or mechanical injury to muscles causes the product of the insulin-like growth factor 1 (IGF-1) gene to undergo alternative splicing, leading to production of a splice variant termed mechano-dependent growth factor (MGF). Previous in vitro experiments have demonstrated increases in the proliferative activity of myogenic precursors on exposure to MGF. However, the question of the physiological effects of MGF in the structures of normal and pathologically altered skeletal muscle remained open. We report here studies of the effects of administration of recombinant full-size MGF into the gastrocnemius muscle of rats during at 30-day recovery period after 16 weeks of alcohol intoxication. Alcoholized rats showed significant decreases in the intensity of proliferation of satellite cells, decreases in the numbers of myonuclei, and decreases in the phosphorylation of p90RSK. Studies of the level of phosphorylation of ribosomal S6 protein kinase p70S6K indicated that there were no significant changes. Administration of MGF increased the proliferative activity of myogenic precursors and restored the pool of myonuclei; the level of phosphorylation of p90RSK was also increased.

The gene xylE encoding endo-1,4-b-xylanase from the 10th family of gly cosyl hydrolases produced by the mycelial fungus Penicillium canescens has been expressed under the control of the strong promoter of the bgaS gene encod- ing b-galactosidase from P. canescens. As a result, a strain-producer of endoxylanase XylE was developed. The recombinant enzyme was isolated and purified to homogeneity with specific activity of 50 U/mg. The physicochemical and biochemical properties of the endoxylanase were studied. The maximal enzymatic activity was observ ed at pH 6.0 and 70°C. Endoxylanase XylE was shown to be a highly thermostable enzyme with half-inactivation period t1/2 of 7 h at 60°C. The kinetic parameters were 0.52 mg/ml (Km) and 75 µmol/min per mg ( Vmax) using birch xylan as the substrate. Crystals of endoxylonase XylE were obtained, and the 3D structure was solved at 1.47 A resolution. The 3D structure of an endo-1,4- b-xylanase from the 10th family containing carbohydrate and unique cyclic structure located at the C-terminus of the polypeptide chain was obtained for the first time.

Ген xylE эндо 1,4-ƒ-ксиланазы десятого семейства гликозил-гидролаз мицелиального гриба Penicillium canescens экспрессирован под контролем сильного промотора гена bgaS, кодирующего ƒ-галактозидазу P. canescens и получен штамм - продуцент эндоксиланазы XylE. Фермент выделен в гомогенном состоянии (специфическая активность 50 ед/мг) и исследованы его физико-химические и биохимические свойства. Максимальная ферментативная активность наблюдалась при рН 6,0 и 70. Эндоксиланаза XylE является вы- сокостабильным ферментом, период полуинактивации фермента ƒ1/2 при 60 равен 7 ч. Кинетические пара- метры, определенные по березовому ксилану, равнялись 0,52 мг/мл (Km) и 75 мкМоль/мин/мг (Vmax). Полу- чены кристаллы эндоксиланазы XylE и решена трехмерная структура с разрешением 1,47 Е. Впервые опре- делена кристаллическая структура эндо 1,4-ƒ-ксиланазы 10 семейства, содержащая углеводы и уникальную циклическую структуру на С-конце.

The gene xylE encoding endo-1,4-β-xylanase from the 10th family of glycosyl hydrolases produced by the mycelial fungus Penicillium canescens has been expressed under the control of the strong promoter of the bgaS gene encoding β-galactosidase from P. canescens. As a result, a strain-producer of endoxylanase XylE was developed. The recombinant enzyme was isolated and purified to homogeneity with specific activity of 50 U/mg. The physicochemical and biochemical properties of the endoxylanase were studied. The maximal enzymatic activity was observed at pH 6.0 and 70°C. Endoxylanase XylE was shown to be a highly thermostable enzyme with half-inactivation period τ1/2 of 7 h at 60°C. The kinetic parameters were 0.52 mg/ml (K m) and 75 μmol/min per mg (V max) using birch xylan as the substrate. Crystals of endoxylonase XylE were obtained, and the 3D structure was solved at 1.47 Å resolution. The 3D structure of an endo-1,4-β-xylanase from the 10th family containing carbohydrate and unique cyclic structure located at the C-terminus of the polypeptide chain was obtained for the first time.

Для получения гидролизатов с ценными биологическими характеристиками проведена оптимизация процесса ферментативного гидролиза кератинсодержащего сырья. Увеличение весового соотношения сырья и воды, количества вносимого ферментного препарата щелочной протеазы С из Acremonium chrysogenum и повышение температуры реакционной смеси приводили к росту выхода продуктов гидролиза и их антиоксиоксидантной емкости. Молекулярные массы основных растворимых продуктов, полученных в оптимальных условиях гидролиза, составляли от 3.55 до 3.60 кДа. Продукты характеризовались высокой антиоксидантной емкостью, 100%-ной перевариваемостью и сбалансированным составом аминокислот.

Optimization of the process of enzymatic hydrolysis of keratin-containing stock aimed at obtaining hydrolysates of high biological value has been performed. The increasing of the stock/water weight ratio, the amount of the alkaline protease preparation from Acremonium chrysogenium added and the temperature of the reaction mixture resulted in an increase in the yield and antioxidant capacity of hydrolysis products. The molecular masses of soluble products obtained under optimal hydrolysis conditions ranged from 3.55 to 3.60 kDa. High antioxidant capacity, 100% bioavailability and a well-balanced amino acid composition was characteristic of the hydrolysis products.

Eight different mouse myostatin small interfering RNA (siRNAs) were synthesized and tested. Five siRNAs showed a pronounced biological effect reducing myostatin mRNA content. For two of them, the myostatin mRNA level was reduced 3-and 4-fold, respectively. The obtained siRNAs can be used for study of biological effects of myostatin, both in vitro and in vivo.

The aim of study was to investigate the effect of oral creatine supplementation upon muscle performance and aerobic capacity of the organism. Knee extensor muscles of two groups with 9 subjects in each were subjected to strength training with and without creatine supplementation (Cre and Pla) for 10 weeks, three times a week with an effort of up to 85% of maximal voluntary contraction (MVC). The Cre group received 5 g of creatine monohydrate a day. After 10 weeks strength training, an increase of MVC by 29 and 40% in training (isotonic) regimen was recorded for the Pla and Cre groups respectively. The muscle isokinetic torque increments of 10-11% were obtained in the Pla group at angular velocities corresponding to training velocities, and in the Cre group increments of 11-17% were recorded at all angular velocities tested. No changes were found in the fatigue test by the Pla group, whereas Cre group showed a tendency for an increase. The aerobic and anaerobic capacities of the organism did not decrease in both groups. Thus the creatine supplementation during strength training potentates an increase of force-velocity characteristics of trained muscle group without impeding aerobic capacity of the organism.