In Cameroon, most of the crude palm oil (CPO) consumed locally is produced by the informal sector and is generally of poor quality. The quality of palm oil is mainly determined by its acidity which is generated by a very active lipase present in the mesocarp of ripe palm fruits. Previous studies showed a strong variability of this trait amongst progenies, and the segregation of forms suggested a monohybridism with dominance of the strong acidity allele. The objective of this study was to get more insights into this mechanism by explaining the phenotypic variability of palm oil acidity (POA) in view of possible production of seeds bearing this low oil acidity trait. Individual palms were grouped in classes based on their level of acidity from the mean and standard deviation. Figures of each class of acidity were compared to the theoretical proportions derived from the normal distribution using Chi square test (χ2) at 5% significance threshold according to the genetic determinism of POA previously demonstrated. POA assessment of 650 palms indicated a strong variability, with values ranging from 0.5 to 42% and an average of 10 ± 8%. The normal distribution of F2 into 3 classes around 1.34 ± 0.6, 15 ± 6 and 21.92 ± 5%, corresponded to the genotypes « papa », « Papa » and « PaPa » respectively conferring low, average and high acidity traits. This suggest the presence of minor genes around the major gene controlling POA, with the dominance of high acidity form.

The aspect of this work is to produce extracellular protease enzyme which could be applicable in Leather industries worldwide. Protease is an extra cellular proteolytic enzyme that hydrolyzes proteins into amino acids. The isolated strain with high protease yields was optimized with respect to growth media, inoculum concentration and agitation speed. Maximum protease production occurred in Wheat flour Skim milk (WS) medium containing Wheat flour, (1%w/v); Skim milk powder, (1%w/v); NaCl (0.5%w/v), and initial inoculum concentration of 6% (v/v) at 140 rpm shaking conditions and at 72 hours. The optimum pH and temperature for protease activity was assayed using casein as a substrate dissolved in buffers with pH ranging from 4.0 to 10.0 at different temperatures from 250C to 750C. The crude protease showed maximum enzyme activity at pH 9.0 in 0.1 M Carbonate-bicarbonate buffer at 400C. This activity was considerably maintained for 1hour. The enzyme exhibited remarkable stability in the presence of SDS and Triton X-100. The application study suggested that the crude enzyme could be effectively used to remove hair from goat skin indicating its potential in Leather processing industry.

Malaria is one disease which is dangerous in tropical world. Pathophysiological process involves centrilobular liver damage due to invading sporozites causing destruction of RBC. Liver and RBC’s are abundant in Lactate Dehydrogenase (LDH), an intracellular enzyme, which is released into the circulation on injury of liver and destruction of RBC. Serum LDH activity is an extremely valuable enzymatic marker of acute malarial patients. Alanine Transaminase (ALT) is found largely in liver, so it serves as a marker of liver damage. RBC contain surplus of Acid Phosphatase (ACP). Similarly, Alkaline Phosphatase (ALP) serves as marker of liver damage. Samples were collected from 68 individuals and Enzymes were assayed on Autoanalyser while ACP was assayed on semi-autoanalyser by Kinetic Method. ). It was detected that enzyme ACP, AST, ALT, ALP activity rises significantly (p<0.05) and increase in LDH is highly significant (p<0.001) in patients with vivax malaria as compared to the control subjects. It was further observed that enzyme AST, ALT, ALP activity increases significantly (p<0.05) and increase in ACP, LDH is highly significant (p<0.001) in falciparum malaria patients as compared to control subjects. The results of the present research provide information and association between hepatic and RBC biochemical derangements in vivax/falciparum malaria patients. Early treatment can be initiated based on these findings to avoid complications and to diminish mortality. These enzymatic markers also have a supportive role in knowing the extent of hemolysis and liver damage and thus the severity of the disease.

Antimicrobial resistance is one of the most pressing issues of modern epoch, according to WHO’s reports of recent decades. In current paper, 6 new synthetic derivatives of natural antimicrobial compound from plant source – L-tartaric acid, were elaborated in National Polytechnic University of Armenia (NPUA). Biological activity and biodegradation potential of benzyl- cyclohexyl- and phenyl- imides and complex mono amino salts of tartaric acid were tested on phytopathogenic Pseudomonas syringae of soil. Due to results, benzyl- and cyclohexyl- complex salts of tartaric acid are more effective then phenyl mono amino salt. As the prospective and a comparably ecologically safe alternative for combating antimicrobial resistance in this plant pathogen P. syringae, complex salts are more effective than the appropriate imide derivatives. The obtained compounds are effective against the other opportunistic pathogenic Pseudomonas (P. aeruginosa, P. fluorescens, etc.). Besides, they are biodegradable by soil non-pathogenic P. chlororaphis group representatives.