SU M M A RYThis study was undertaken to determine the antidiabetic and antioxidant effects of oral administration of ethanolic extract of Moringa oleiferaflower on stretozotocin-induced diabetic rats at 100, 200, and 300 mg/kg b.w. Thirty (30) male experimental albino rats were grouped randomly into six groups: groups A, B, and F are the control, diabetic control and reference drug groups, while C-E received 100, 200, and 300mg/kg b.w of the extract, respectively. Blood samples and organs were collected to assay for blood glucose level and antioxidant enzymes.Levels of blood glucose, serum lipids and lipid peroxidation as well as aspartate aminotransferase (AST), alkaline phosphatase (ALP), and alanine aminotransferase (ALT) activities were significantly reduced (p<0.05) in STZ-induced diabetic rats orally administered ethanolic extract of M. oleifera flower. However, the body weight; catalase and superoxide dismutase activities were significantly increased (p < 0.05) when compared with the controls.M. oleifera flower ethanolic extract administered orally therefore exhibited improved lipid metabolism, glucose-lowering potential and is hence beneficial in preventing diabetic complications as a result of lipid peroxidation and oxidative systems in streptozotocin-induced diabetic rats. It could thus be employed therapeutically in managing diabetes mellitus.

Peroxidase from Eichhornia crassipes leaf was purified 23.58 fold with 18.58% yield by means of (NH 4 ) 2 SO 4 precipitation, ion exchange and Sephadex G-75 gel filtration chromatography. Optimum temperature and substrate-dependent pH optimum for enzyme activity were 40 °C and pH 4.0, 9.0 and 6.0 for 2,2'-azino-bis-(3-ethylbenzthiazolin)-6-sulfonate (ABTS), guaiacol and pyrogallol, respectively. The enzyme had high pH stability and moderate thermal stability at temperatures up to 60 °C; the activation energy of inactivation of the enzyme was ~122.29 kJ mol -1 . Temperature-denaturing and spontaneous recovery were shown to be time-dependent while Ca 2+ -enhanced recovery of the denatured enzyme was in a time-dependent manner. The enzyme showed preferential affinity for ABTS over guaiacol and pyrogallol with K M values of 31.11, 21.91 and 6.45 mM respectively. It was reversibly inhibited by Pb 2+ , Hg 2+ and EDTA while urea only caused loss of ~30.40% activity after 60 min of incubation. E. crassipes leaf peroxidase has potential use for broad range of applications.

Summary So far, some prospective metal-based anti-malarial drugs have been developed. The mechanochemical synthesis and characterization of Zn (II) complex with amodiaquine and its anti-malarial efficacy on Plasmodium berghei-infected mice and safety evaluation were described in this study. Solvent-free mechanochemical synthesis and characterization of Zn (II) complex with amodiaquine as well as its anti-malarial efficacy on NK-65 Plasmodium berghei-infected mice and safety were evaluated. Derivatization of amodiaquine with zinc (II) ion enhanced the activity of the drug through significant (p < 0.05) enhancement of parasitemia suppression in established malaria infection in comparison with the controls, while its capacity to clear malaria parasite was similar to that of chloroquine. A significant reduction in the liver, kidney and small intestinal activities of alkaline phosphatase, lactate dehydrogenase and alanine and aspartate aminotransferases was observed, while their levels increased significantly in the plasma. Levels of PCV, Hb, RBC and lymphocytes were significantly reduced (p < 0.05), and significant elevation (p < 0.05) in WBC and neutrophil concentrations across all the treatment groups when compared with control was observed. The result indicates that coordination of zinc (II) to amodiaquine by mechanical induction improved its anti-malarial activity, while the alterations in the investigated biochemical parameters suggest functional and structural toxicity. Thus, Zn (II) complex with amodiaquine may not be completely safe for prolonged and repeated use as an oral anti-malarial remedy.

The antimalarial efficacy and safety of mechanically induced solventlessly synthesized lumefantrine-copper complex were investigated in experimental mice. Parasite level in Plasmodium berghei-infected mice treated with lumefantrine -copper complex (LCC) significantly declined (p < 0.05) at day 3 and was comparable with that of chloroquine-treated mice. LCC attained a percentage chemo-suppression which was significantly higher than those of pure lumefantrine and comparable with chloroquine. Pure lumefantrine attained a clearance of 88.52%, chloroquine was 91.95%, while LCC was 95.10%. Administration of lumefantrine, LCC and chloroquine to mice for 7 days caused a significant increase (p < 0.05) in the activities of alkaline phosphatase, acid phosphatase and lactate dehydrogenase in the liver when compared with the control, and a significant reduction (p < 0.05) in the liver and kidney activities of alanine and aspartate aminotransferases when compared with the control. Also, there was a significant decrease (p < 0.05) in the levels of PCV, Hb, RBC and lymphocytes and a significant increase (p < 0.05) in the white blood cells count and neutrophil counts in all the treatment groups when compared with control. Alterations in the biochemical parameters and chromosomal aberration in the organs investigated suggested selective, chromosomal and functional toxicity of the tested drugs.Keywords: chloroquine, chromosomal aberration, lumefantrine-copper complex, malaria, solvent-less synthesis Abbreviations: ALT -alanine aminotransferase, AST -aspartate aminotransferase, b.wt. -body weight, LCC -lumefantrinecopper complex, PCV -packed cell volume, Hb -haemoglobin level, WBC -white blood cells count, RBC -red blood cell count, MCV -mean corpuscular volume, MCH -mean corpuscular, TNMA -total number of metaphases analysed, MCAmetaphases with chromosomal aberration, MI -mitotic index, CA -chromosomal aberration Available online: www.notulaebiologicae.ro

Background: Agrowastes like Theobroma cacao (Cocoa) pod husk can be used to prepare bioactive peptides with various bio-functionalities. Objectives: This study aimed to investigate antioxidant and angiotensin converting enzyme I (ACE) inhibitory peptides contained in Theobroma cacao (cocoa) pod husks – an agro-waste. Methods: Protein isolated from cocoa pod husk was enzymatically digested with alcalase, pepsin, and trypsin. ACE inhibition, kinetics of ACE inhibition, and antioxidant properties of the cocoa pod husks hydrolysates were evaluated in vitro. Results: Trypsin and alcalase hydrolysates displayed higher peptide yields (63.1% and 61.2%) than pepsin hydrolysate (61.2%). However, no significant difference (P>0.05) was observed in the degree of hydrolysis (DH) of the three proteases on cocoa pod husk protein. Methionine, lysine, and cysteine were the amino acid residues presented in cocoa pod husk hydrolysates. A concentration-dependent ACE inhibition by cocoa pod husk hydrolysates was observed. The highest ACE inhibitions of 84.4%, 81.5%, and 73.5% were obtained at 2.0 mg/mL of pepsin, trypsin, and alcalase hydrolysates, respectively, with the minimum IC50 value of 0.36 mg/mL obtained for trypsin hydrolysate. An uncompetitive and mixed-type inhibition was obtained from double reciprocal plots of alcalase and pepsin as well as trypsin cocoa pod husk protein hydrolysates. The Ki values of ACE inhibition for pepsin, trypsin, and alcalase hydrolysates were 3.05, 2.19, and 3.57 mg/mL, respectively. A concentration-dependent increase in the scavenging of 2,2-diphenyl-1-picrylhydrazyl and superoxide radicals as well as ferric reducing antioxidant power were recorded for the cocoa pod husk hydrolysates. Conclusion: Trypsin and alcalase cocoa pod husk protein hydrolysates could be an effective source of a natural ACE inhibitor and antioxidant.