Chemical Composition and Biological Activity of Ver-Mol-2 Camel Milk
Camel milk and shubat, a lactic fermentation product, are used in folk medicine and several clinics in Kazakhstan to treat tuberculosis, chronic gastritis, colitis, and other diseases and to improve in vivo protective forces. However, the chemical composition and biological properties of Ver-Mol-2 are insufficiently studied for this purpose. The goal of the present investigation was to study the chemical composition and biological properties of Ver-Mol-2, which is produced from camel shubat. The experiments used lyophilized Ver-Mol-2. The amino-acid composition was determined chromatographically using a Beckman System Gold high-pressure chromatograph, integration by an IBM 286, and Gold program version 3.10. The column was an Ultrasphere C-18. The eluent was 50% MeCN in H2O (B) with a linear gradient of B and A from 2 to 80%. Detection was made at 254 nm with sensitivity 0.01. The standard was an amino-acid mixture (Sigma, USA). The trace-element composition of Ver-Mol-2 was determined by neutron activation at the Institute of Nuclear Physics, AS, RU; hypoglycemic properties, in alimentary and adrenaline hyperglycemia models. The blood sugar (glucose) level was measured 1 h after inducing hyperglycemia. The blood-serum sugar contents were determined using glucose oxidase and a BioGlucoFen kit (IBOC, AS, RU). Alimentary hyperglycemia was induced by feeding rats glucose at a dose of 9 g per kg of body mass using a stomach catheter; adrenaline hyperglycemia, by injecting adrenaline (50 g/kg, i.p.) 1 h before drawing blood [1]. The control animals received orally distilled H2O (1 mL). A total of 18 amino acids were detected in the Ver-Mol-2 protein hydrolysates (Table 1). Table 1 shows that the total and free amino acids contained all essential amino acids, i.e., valine, methionine, isoleucine, leucine, lysine, phenylalanine, histidine, and arginine. Elevated amounts of glutamic acid (12.6%), alanine (7.8%), lysine (7.0%), tyrosine and valine (6.1%), phenylalanine (6.3%), and isoleucine (6.6%) were characteristic of all lactic fermented products, including Ver-Mol-2. Ver-Mol-2 was a product of mixed lactic and alcoholic fermentation [2]. The increased contents of free amino acids during aging of Ver-Mol-2 was evidently explained by cleavage of part of the starting milk proteins by proteolytic enzymes, i.e., stimulators of lactic and alcoholic fermentation to free amino acids. In addition to these proteolytic processes, proteins were resynthesized by the lactic and alcoholic fermentation stimulators. This could be seen in the change of free-amino-acid contents in Ver-Mol-2 as compared with raw milk. The amount of free amino acids, especially non-essential ones (glutamic acid, alanine, proline) and essential ones (tyrosine, valine, cysteine, phenylalanine, histidine) increased during fermentation of Ver-Mol-2. The trace-element composition of Ver-Mol-2 was determined by neutron activation. The results are presented below:
Camel Milk : A Boon to Mankind
This paper embraces most of the medical benefits of camel milk. It is far better than cow milk and most of its contents and properties resemble to those of mother’s milk. It has low fats, have insulin-like and protective protein and have lactose as the major carbohydrate. It can be used for the treatment of many ailments like diabetes, autism, diarrhea, it possesses anti-tumors properties and the potent immune system components help fight diseases. Due to these qualities it has been utilized for ages by the nomads and Bedouins.
New method for analysis of enzymatic reactions: Thermolysin-catalyzed synthesis of aspartame precursor
Aspartame is an artificial sweetener which is 200 times sweeter than sucrose. A precursor of aspartame, N-(benzyloxycarbonyl)-l-aspartyl-l-phenylalanine methyl ester (Z-APM) was synthesized and hydrolyzed with thermolysin in an aqueous monophasic system. Graphical plotting methods and/or nonlinear regression have been used to analyze enzymatic reactions because of the nonlinearity of enzymatic rate equations. There are, however, problems: the former require accurate measurement of the initial reaction rate and the latter gives no analytical information. The authors proposed a method to solve the nonlinear enzymatic rate equations with respect to the concentration of a product with the Taylor expansion, especially for the reversible Theorell-Chance mechanism (Murakami, Y., Hirata, M., and Hirata, A., J. Ferment. Bioeng., 82, 246–252, 1996). This solution, however, is complex for practical use. In this paper, a simpler solution to explain the thermolysin-catalyzed synthesis of Z-APM is obtained. New methods to determine the kinetic parameters, especially for the reversible Theorell-Chance mechanism, based on the approximated solution are proposed. The results calculated using the obtained kinetic parameters can satisfactorily explain the experimental results, which demonstrates the effectiveness of the proposed analysis. We must know the relation between the concentrations of substrates and a product, and accurately evaluate of the result obtained using Taylor expansion when we determine the kinetic parameters using our newly developed methods. The methods to determine the kinetic parameters of the reversible Theorell-Chance mechanism described in this paper is, however, expected to be applied to general enzymatic reactions.