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Copyright of Revista Colombiana de Ciencia Animal - RECIA is the property of Revista Colombiana de Ciencia Animal - RECIA and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The objective of this work was to evaluate the perspectives of the use of Trichoderma spp. for the management of chickpea wilt caused by Fusarium oxysporum f. sp. ciceris. The main aspects related to the antagonistic and mycoparasitic activity of Trichoderma spp. are summarized, as well as the enzymatic machinery deployed in the microorganism-microorganism interaction. A model integrating the different stages of the mycoparasitic activity of Trichoderma against Fusarium is proposed, based on the results of the T. harzianum -Th 4 interaction on Fusarium oxysporum f. sp. ciceris-1 and the specialized literature on the subject. Autochthonous Trichoderma strains show mycoparasitic activity against Fusarium oxysporum f. sp. ciceris, suggesting their potential use in the management of chickpea wilt. [ABSTRACT FROM AUTHOR]

Mycoparasitic fungi are capable of hydrolyzing the cell walls of their host by secreting hydrolytic enzymes, such as proteases. To quantify proteolytic activity, the methodology based on the use of the azocasein substrate is considered one of the most reliable methodologies. However, in the literature it has multiple modifications available according to its applicability and the type of microorganism. Therefore, this work was aimed to establish the optimal reaction conditions using the papain pure enzyme; in order to quantify the proteolytic activity of fungal enzyme supernatants from Trichoderma and Escovopsis. The effect of reaction time, pH, and temperature over enzymatic activity at different concentrations of papain was tested. The chromogenic substrate azocasein was used to measure the enzymatic activity. Enzyme supernatants were obtained by liquid fermentation of two fungal mycoparasites: Escovopsis HEP25 and Trichoderma POS7. According to the evaluated conditions, significant proteolytic activities were observed at 50 min of reaction, 37 °C and pH 7.4.The activity was expressed in terms of units equivalent to the activity of a given mass of papain (1 unit = 1 mg of papain). For the Trichoderma strain (POS7) an activity of 54.3 ± 2.8 U/L was obtained, and for the Escovopsis strain (HEP25) of 2 ± 0.5 U / L. The adjusted methodology and the enzyme activity calculation were determined to be appropriate for analyzing the crude supernatant samples. Particularly, for the Escovopsis genus, the determination of quantitative proteolytic activity is reported for the first time. [ABSTRACT FROM AUTHOR]

The normal process of obtaining chitin from the shrimp exoskeleton consists in associated compounds extraction through successive steps of demineralization, deproteinization and depigmentation, using strong acids and alkalis. It constitutes a risk for personal and environmental integrity. A solution to this problem is the alternative methods use, such as enzymatic extraction, which in addition to maintain the structure of chitin intact, do not produce wastes that may affect their biomedical applications. The exoskeleton, once clean, dry and ground to 300 μm, is demineralized, up to 95,67% using glacial acetic acid at 15% at room temperature and stirring for 3 hours. A treatment with α-chymotrypsin in an enzyme-substrate ratio E / S 0,7: 100 (QB2) shows a higher percentage of protein hydrolysis, 73,48% than the E / S ratio 0,5: 100 (QB1) . However, it was found that there is not statistically significant difference between the different treatments, only a difference between the QB1 and QB2 treatments was observed, which seems to indicate which seems to indicate that a greater deproteinization of the substrate occurs at a higher concentration of chymotrypsin.On the other hand, papain treatments reached similar percentages of deproteinization, 65,43% and 67,13% for E/S ratios of 0,5: 100 and 0,7: 100 respectively, which indicates that both treatments are statistically acceptable. Regarding the degree of deacetylation, all the treatments showed a value of approximately 20% and a molecular mass of the order of 106, thus demonstrating the effectiveness of the combination of treatments with weak acids and proteolytic enzymes. [ABSTRACT FROM AUTHOR]

Enzymatic activity of proteases from Cyprinus carpio (Cypriniformes: Cyprinidae) captured in a polluted lagoon in Mexico. Common carp (Cyprinus carpio) is an aquatic organism of commercial value able to survive in polluted environments; carps contain proteolytic enzymes of physiological importance and potential industrial application. The objective of this work was partially purify and study the proteolytic activity at different pH of carp proteases living in a polluted environment. Three carps were captured in different zones of Zumpango polluted lagoon (Mexico) at 1 m of maximum deep. Protease crude extracts were obtained from dorsal muscle by aqueous extraction and fractionated by 20 %, 50 %, 80 %-saturated (NH4)2SO4. Fractions extracted with 50 % and 80 %-saturated (NH4)2SO4 were selected for their high proteolytic activity and concentrated by ultrafiltration through 100 kDa molecular weight cutoff membranes and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The crude proteolytic extract had significantly higher activity (19.7 - 20.3 U / mg) at pH 2, 5, and 7 (P < 0.001). Fractions obtained with 20 %, 50 % and 80 % - saturated (NH4)2SO4 showed peak activity at pH 5 (2.8 U / mg) and pH 6 (2.2 U / mg); pH 6 (4.3 U / mg) and pH 3 - 4 (3.6 - 3.7 U / mg); pH 3 (10.8 U / mg) and pH 10 (10.6 U / mg); respectively. Subfractions of < 100 kDa, obtained with 50 % and 80 %-saturated (NH4)2SO4, had peak proteolytic activity at alkaline pH. A < 100 kDa fraction, obtained with 80 %-saturated (NH4)2SO4, had the highest proteolytic activity (37.3 - 43.7 U / mg) at pH 8 - 10, purification factor of 3 and 19.1 % recovery. Thirteen proteins between 9.8 to 104.8 kDa were identified in the crude extract. Peak protein concentration was observed for 31 - 33 and 39 - 41 kDa, suggesting the possibility predominance of serine- and aspartyl- proteases, respectively. We suggest this protease with maximum activity at alkaline pH is related to the adaptation of C. carpio to polluted waters with high pH. Although unsuitable for human consumption, these organisms can be a source of protease production aimed to several uses as in the industry and waste water treatment among others. [ABSTRACT FROM AUTHOR]

Copyright of Medicina (Buenos Aires) is the property of Medicina (Buenos Aires) and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Revista Colombiana de Biotecnología is the property of Universidad Nacional de Colombia and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Muscle waste in cancer cachexia, proteolytic mechanism The cachexia associated to neoplasm is a syndrome characterized by a remarkable loss of weight, anorexia, loss of muscle mass and anemia. In fact, a high percentage of patients who die of advanced cancer show cachexia. The cachexia condition is associated with the presence and the growth of tumor that produces a condition of malnutrition as a consequence of anorexia. On the other hand, the metabolic disorders and the competence for nutrients between tumoral and normal cells induce an accelerated condition of wear out of patients. Though, it is certain that this accelerated wear out is caused by anorexia and the metabolic disorders that produce the hypermetabolism, all together explain to a great extent the events present in this syndrome however, the molecular disfunctios cannot be left aside. In this sense the proteolytic system is of great importance, in animal models with developed tumors as in patients with cancer, it is observed an increase in the expression and activity of the proteolyses system; both, lysosomal and non lysosomal, in particular the proteolytic system dependent of ATP and ubiquitin "proteasome". [ABSTRACT FROM AUTHOR]

A safe conservation method not affecting the strain characteristics is essential for developing any microorganism as a potential biological agent. The serial subculture is one of the most used methods. The aim of this work was to find out the effect of this practice on protease production by the strain IMI SD 187 of the nematophagous fungus Pochonia chlamydosporia var. catenulata. The study was carried out on solid medium by measuring the gelatine degradation halo, the fungal growth and the PA indicator (protease activity) at different days after inoculation. Adverse effects of serial subculture on protease production by the strain studied were not observed confirming the robustness of this strain. [ABSTRACT FROM AUTHOR]

The detection of protease production is an important aspect for selecting some biological control agents, because of the role these enzymes play in the infectious process. The aim of this work was to modify a method for detecting proteases in solid medium supplemented with gelatine, using different dyes and measuring the gelatine degradation halo, the colony growth and the protease activity (PA) indicator. Trypan blue at 0.03% was the most efficient alternative with a good visualization of the degradation halo and the least effect on the fungal colony growth. [ABSTRACT FROM AUTHOR]

Copyright of Boletin Intexter del Instituto de Investigacion Textil y Cooperacion Industrial Terrassa is the property of Universitat Politecnica de Catalunya and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)