Rosemary leaves extract: Anti-snake action against Egyptian Cerastes cerastes venom

The morbidity caused by viper bites is very dangerous and the anti-venom therapy couldn't treat the local injures such as hemorrhage, edema, necrosis and inflammation of bitten tissues. Searching for safe and effective anti-venom compounds from natural sources is very important. This study was designed to explore the neutralizing ability of Rosmarinus officinalis L. leaves aqueous extract (RMAE) against Egyptian Cerastes cerastes (Cc) viper venom toxicity. The RMAE contained a considerable amount of phenolic and flavonoid contents with 3,300 and 800 mg/100 g dry weight, respectively. The RMAE showed a considerable variation of phenolic acids by using HPLC technique. Rosmarinic acid is the major component of the RMAE which recorded 400 mg/100 g dry weight and 64% of all the identified compounds. In vitro, the RMAE neutralized the enzymatic activities of proteases, l-amino acid oxidases, and phospholipases A2 of the Cc venom dose-dependently. In addition, the RMAE effectively neutralized the gelatinolytic, fibrinogenolytic, hemolytic and procoagulant activities of Cc venom. In vivo, the RMAE markedly reduced lethality, hemorrhage, edema, muscle and liver toxicities induced by Cc venom. In conclusion, the venom neutralizing property of the RMAE gives a new prospect for efficient treatment of the lethal viper bites. Keywords: Cerastes cerastes, Venom, Enzymes, Lethality, Rosmarinus officinalis L., Neutralizatio

Synthesis and Antimicrobial Activity of Some New Benzimidazole Derivatives

Reaction of 3-(2-methylbenzimidazol-1-yl)propanoic acid hydrazide (1) with CS2/KOH gave oxadiazole 2 which underwent Mannich reaction to give 3. Compound 2 was treated with hydrazine hydrate to give triazole 4 which was treated with both aldehydes and acetic anhydride to give 5 and 6, respectively. Carbohydrazide 1 was reacted with ethyl acetoacetate, acetylacetone and aldehydes to give 7, 8 and 9, respectively. Cyclocondensation of 9 with thioglycolic and thiolactic acids gave 10 and 11, respectively. Some of these compounds showed potential antimicrobial activities

Purification and characterization of deoxyribonuclease from small intestine of camel Camelus dromedarius

The chromatography of deoxyribonuclease (DNase) from small intestine of camel Camelus dromedarius by DEAE-Sepharose separated three isoforms DNase 1, DNase 2 and DNase 3. The DNase 3 was purified to homogeneity by chromatography on Sephacryl S-200. The molecular weight of DNase 3 was 30 kDa using gel filtration and SDS-PAGE. The pH optimum of DNase 3 was reported at 7.0 using Tris-HCl buffer. The temperature optimum of DNase 3 was found to be 50 °C. The enzyme was stable up to 50 °C for one h incubation. The Km value was 28.5 µg DNA, where this low value indicated the high affinity of enzyme toward DNA as substrate. No activity of DNase 3 was determined in the absence of metal cations. Mg2+ and Ca2+ caused significant enhancement in the enzyme activity by 90 and 75%, respectively. The mixture of Mg2+ and Ca2+ caused 100% of enzyme activity. Ni2+, Co2+, Ba2+, Zn2+ and Cd2+ showed very strong inhibitory effect on enzyme activity. In conclusion, the characterization of DNase 3 indicated that the enzyme is considered as a member of DNase I family. The low Km value of the DNA suggested that the high digestion of DNA of camel forage by small intestine DNase 3

Characterization of two thermostable inulinases from Rhizopus oligosporus NRRL 2710

Two inulinases (Inu2 and Inu3) were purified from Rhizopus oligosporus NRRL 2710 by chromatography on DEAE-Sepharose and Sephacryl S-200 columns. The molecular weight of Inu2 and Inu3 were determined to be 76 and 30 kDa, respectively. Inu2 and Inu3 had the same pH optimum at 5.0, temperature optimum at 50 and 60 °C, and thermal stability up to 60 and 70 °C for 1 h, respectively. Inu2 and Inu3 had low km values (0.93 and 0.70 mM, respectively) indicating the high affinity toward inulin. Mg2+, Ca2+, Zn2+ and EDTA did not significantly influence the enzyme activity. Ni2+, Cu2+, Fe2+ and Co2+ showed a partial inhibitory effect, and Hg2+ had a strong inhibitory effect. p-Chloromercuribenzoate had a partial inhibitory effect on Inu2. From these findings, R. oligosporus inulinases can be beneficial enzymes for industrial enzymatic production of high fructose syrup

Development of novel delivery system for nanoencapsulation of catalase: formulation, characterization, and <i>in vivo</i> evaluation using oxidative skin injury model

<p>One of the main challenges for successful pharmaceutical application of Catalase (CAT) is maintaining its stability. Physical immobilization of CAT through nano-encapsulation was proposed to resolve this challenge. CAT encapsulating niosomes (e-CAT) were prepared using Brij^® 30, 52, 76, 92, and 97 in the presence of cholesterol (Ch) by thin film hydration method. Niosomes were characterized for encapsulation efficiency % (EE), size, poly-dispersity index (PI), and morphology. Kinetic parameters, pH optimum, thermal stability, and reusability of CAT were determined. The influence of optimized e-CAT dispersion onto thermally injured rat skin was evaluated. Results revealed that encapsulation enhanced CAT catalytic efficiency (<i>V</i>_max/<i>K</i>_m). Free CAT and e-CAT had pH optimum at 7.0. e-CAT exhibited improved thermal stability where it retained 50% residual activity at 60 °C. Free CAT lost its activity after three consecutive operational cycles; however, e-CAT retained 60% of its initial activity following 12 cycles. After 24 h of topical application on thermal injury, a significant difference in lesion size was observed with e-CAT compared with the control group. Based on these encouraging results, CAT immobilization demonstrated a promising novel delivery system that enhances its operational stability. In addition, nano-encapsulated CAT can be anticipated to be beneficial in skin oxidative injury.</p

Purification and characterization of pectin methylesterase isoenzymes from orange peel

No Abstract. The Egyptian Journal of Biochemistry and Molecular Biology Vol. 24(1) 2006: 73-9