Search

Copyright of Journal of Advanced Research in Health Sciences (JARHS) / Sağlık Bilimlerinde İleri Araştırmalar Dergisi (SABİAD) is the property of Journal of Advanced Research in Health Sciences (JARHS) 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.)

In the study, freeze-dried white mulberry pulp (10%) and leaf (3%) were used in the production of powdered bread wheat flour and whole wheat flour bread. Total amount of phenolic substances was determined as the highest and lowest 48.26±5.40 mg/100 g GAE, 18.50±1.36 mg/100 g GAE in mulberry leaf whole wheat flour and mulberry leaf bread wheat flour, respectively. Bread variety with the highest antioxidant activity was the whole wheat flour bread with mulberry leaves value of 3.29±0.33 µM TEAC/g. Antidiabetic activity, highest and lowest α-glycosidase and α-amylase enzyme inhibition were detected in whole wheat flour with mulberry leaves and bread wheat flour. α-glycosidase and α-amylase enzyme inhibition values of acarbose were found to be 69.00% and 78.30%. It was concluded that white mulberry leaves and whole wheat bread with mulberry leaves could be appropriate for the purpose as an alternative to the diabetics' drug with acarbose active ingredient. [ABSTRACT FROM AUTHOR]

Bioactive flavonoids are considered to be the most important phytochemicals in food that provide many biological benefits for human beings. They have many pharmacological activities that include antioxidant, anti-bacterial, anti-cholinergic, anti-diabetic, anti-mutagenic and anti-inflammatory properties. Morin, a member of flavonoids, exhibit many therapeutic properties by interacting with nucleic acids, enzymes and protein. In this study, morin as natural a phenolic compound showed inhibitory effects against human carbonic anhydrase (CA) isoforms I and II (CA I and II), acetylcholinesterase (AChE) and α-glycosidase enzymes. This phenolic compound was tested for the inhibition of CA I, CA II, AChE, and α-glycosidase enzymes and demonstrated efficient inhibition profiles with Ki value of 31.89 ± 9.07 nM for CA I, 49.25 ± 12.85 nM for CA II, 184.67 ± 30.37 nM for AChE, and 16.99 ± 4.40 nM for α-glycosidase, respectively. [ABSTRACT FROM AUTHOR]

Because of its biocompatibility and degradability to non-toxic products, polylactic acid (PLA) based polymers and copolymers have been employed in novel applications, such as absorbable bone plates, artificial skin, tissue scaffolds, and carriers of drugs for controlled release systems. Enzymatic polymerization using lipase has been receiving much attention as one of the new methodologies that provide biodegradable polymer synthesis without toxic catalysts. Lipases are the most versatile biocatalysts because they can be applied to the synthesis of a wide range of substrates with a high stereospecificity and enantioselectivity. In general lipases used in polyester synthesis are of mammalian (Porcine pancreatic lipase (PPL)), fungal (Candida antarctica lipase B (CAL)), or bacterial origin (Pseudomonas cepacia (PCL)). The hydrolytic degradation of PLA polymers has been extensively investigated. It is now well know that degradation of macroscale PLA devices is heterogeneous: it is faster inside than at the surface. This phenomenon has been assigned to an internal autocatalytic effect of carboxyl end groups. Biodegradation of PLA polymers in soil under natural conditions has also been examined. It was reported that degradation by-products resulting from the hydrolytic degradation can be totally assimilated by microorganisms such as fungi, bacteria, or earthworms, thus indicating that PLA polymers are environmentally benign materials. Hydrolysis reactions may be catalyzed by enzymes known as hydrolases, which include proteases, esterases, glycosidases, and phosphatases, among others. This class of enzymes comprises cell-derived proteins that are responsible for the catalysis of several reactions in the human body. The degradation of PLA in the presence of enzymes has been investigated by many groups. Early in 1981, it was found that proteases showed strong effects on PLLA degradation. In this work, polylactic acid was prepared by lipase catalyzed ring opening polymerization of lactide. Enzymatic polymerization was performed with Candida cylindracea lipase, enzyme and the effect of enzyme concentration, temperature and time parameters on polymerization mechanisms were investigated in detail. A typical procedure for the polymerization of lactide using Candida cylindracea lipase is described as follow. To a mixture of lactide (2.50 mmol) and toluene (0.72 mL) at 80 and 100°C was added Candida cylindracea (2 and 4 wt.-%) under nitrogen atmosphere at different time (1-7 days). After the reaction, the enzyme was removed by filtration and the polymer was isolated by precipitation in choloform. Then degradation mechanisms were examined. PLLA films were prepared using a solvent casting method. One gram of PLLA was dissolved in 20 mL of chloroform while mixing vigorously at room temperature. The dissolved solution was poured onto a leveled Teflon film coated glass plate, spread evenly with a bent glass rod and then allowed to dry for about 24 h at room temperature. The resultant film was peeled from the casting surface. Each of polymeric films were placed in test tubes and dipped in 5 mL of DSM protease solution (50 mM Tris-HCl buffer, pH 8.6). The test tube was sealed and kept constant at 37°C for a predetermined period and enzyme solutions were added every 48 h so that enzyme activity remained at a desired level throughout the experiment. The time course of the weight loss and enzymatic degradation were evaluated and the appearance of the samples was examined. It was found that the L-lactide was polymerized in bulk by Candida cylindracea lipase between 3 and 7 days, in a temperature range 80-100°C to yield the polylactide with an Mw of up to 69800 g.mol-¹. Both the conversion and Mw of the resultant polymeric fraction increased with increasing reaction time 3 days to 7 days respectively at constant lipase concentrations. The chemical structures of the degraded polymer samples were characterized using DSC, FTIR and XRD. The molecular weight of the polymer samples after enzymatic degradation process with protease DSM, decreased 25% after 2 months degradation period. PLA polymers investigated in this study showed degradation as illustrated by the decrease in molecular weight, disappearance of amorphous phase and formation of micro fractures and acicular structures. After detailed evaluation of biocompatibility and toxicity of PLAs, it is expected that they will take the petroleum-based plastics' place in future. [ABSTRACT FROM AUTHOR]