China
Africa
Explore chapters and articles related to this topic
Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Amylases are enzymes that help to convert complex carbohydrates like starch into simple sugars. They are divided into three groups: alpha-amylase, beta-amylase, and gamma-amylase. γ-amylase, is most effective in acidic conditions. Recently, researchers have discovered extracellular amylase-producing terrestrial bacteria like Saccharomycopsis, Arxula adeninivorans, Candida japonica, Saccharomycopsis, Lipomyces, Filobasidium capsuligenum, and Schwanniomyces.
Tropical Herbs and Spices as Functional Foods with Antidiabetic Activities
Published in Megh R. Goyal, Arijit Nath, Rasul Hafiz Ansar Suleria, Plant-Based Functional Foods and Phytochemicals, 2021
Arnia Sari Mukaromah, Fitria Susilowati
Alpha-amylase inhibition assay is commonly used to determine antidiabetic activity. According to the research, clove essential oil exhibits maximum anti-diabetic activity at 100 ug mL−1, whereas clove essential oil emulsion (essential oil (25%) + tween 80 (75%) + ethanol (25%) + water (25%)) shows a maximum anti-diabetic capability (as much as 95.30% inhibition of α-amylase activity) [103]. In addition, clove is an excellent functional food and is appropriate for alternative therapeutic of type-2 DM, because it can prevent activity of key enzymes in type-2 diabetic patients, such as: a-amylase and a-glucosidase [1].
Ameliorating Insulin Signalling Pathway by Phytotherapy
Published in Mahendra Rai, Shandesh Bhattarai, Chistiane M. Feitosa, Ethnopharmacology of Wild Plants, 2021
To be proven potential anti-hyperglycemic agents of T. cordifolia leaves against alpha amylase enzyme. Shareef et al. (2014) had extracted leaves in petroleum ether, chloroform, ethyl acetate and methanol solvents. The percentage inhibition of α-amylase by the extracts was studied in a concentration range of 10–640 μg/mL. Of the four extracts, ethyl acetate and methanol were comparatively effective than in petroleum ether and chloroform in inhibiting α-amylase. The IC50of petroleum ether and chloroform extract was 100 and 120 μg/mL, respectively, and methanol extracts were 20 μg/mL. The ethylacetate and methanol exhibited a maximum inhibition of 98% at 50 μg/mL concentration. Dinesh Kumar et al. (2010) had performed in vitro assay by taking ethanolic extract against α-amylase at concentrations 10–100 μg/mL, which exhibited minimum alpha-amylase inhibitory effects from 12.32 ± 0.79 to 36.41 ± 0.39 μg/mL with an IC50 value 138.80 ± 0.16 μg/mL. Dichloromethane (DCM) extract demonstrated 100% inhibition of the α-glucosidase (Chougale et al. 2009), but in the case of, salivary amylase and pancreatic amylase were 75% and 83%, respectively. Introducing maltose load of 2 mg/g along with 0.3 mg/g b. w. of the DCM stem extract to the normal and diabetic rats, the hypoglycemic activity was raised by 50 and 58%, respectively, as compared to the controls. The extract happened to inhibit α-glycosidase in a non-competitive way.
Lower activity of salivary alpha-amylase in youths with depression
Published in Stress, 2020
Daniela Jezova, Jana Trebaticka, Katarina Buzgoova, Zdenka Durackova, Natasa Hlavacova
Lower alpha-amylase activity in youths with depression as compared to that in healthy controls was unexpected with respect to the hypothesis postulated. As the alpha-amylase activity has not yet been investigated in this context, the present data cannot be directly confronted with previous studies. The majority of the present sample was newly diagnosed adolescents and consistently, lower alpha-amylase activity was observed in drug-naive adult patients with first episode of depression compared to healthy subjects (Szarmach et al., 2017). The present finding is consistent also with the results obtained in anxious healthy prepubertal children exhibiting lower alpha-amylase activity compared to non-anxious children (Kapsdorfer et al., 2018). Thus, the low alpha-amylase activity revealed in this study may be related to age scope studied as well as to the presence of patients with mixed anxiety-depressive disorder in the present sample.
Higher perceived stress is associated with lower cortisol concentrations but higher salivary interleukin-1beta in socially evaluated cold pressor test
Published in Stress, 2020
Katarina Buzgoova, Lucia Balagova, Martin Marko, Daniela Kapsdorfer, Igor Riecansky, Daniela Jezova
The present results demonstrate that the time course of changes in alpha-amylase activity throughout the socially evaluated CPT is different in low and high stress perception groups. We failed to observe a strong stress-induced elevation of alpha-amylase activity described previously (Sanger, Bechtold, Schoofs, Blaszkewicz, & Wascher, 2014). However, the mentioned authors performed the socially evaluated CPT differently, namely by immersion of the forearm, excluding the hand, to ice water for 3 min (or until they could no longer tolerate it). The present results are consistent with the data of Giles, Mahoney, Brunyé, Taylor, and Kanarek (2014) who did not observe elevation of alpha-amylase activity in response to socially evaluated CPT in healthy subjects (but without taking into account the degree of stress perception). These authors reported higher values of alpha-amylase before the test compared to the values in a non-stressed control group. In the present investigation, alpha-amylase activity decreased immediately after hand withdrawal and then returned back to initial values though with a different dynamics in the groups.
In silico assessment of potential leads identified from Bauhinia rufescens Lam. as α-glucosidase and α-amylase inhibitors
Published in Journal of Receptors and Signal Transduction, 2021
Wadah Osman, Esraa M. O. A. Ismail, Shaza W. Shantier, Mona S. Mohammed, Ramzi A. Mothana, Abdelkhalig Muddathir, Hassan S. Khalid
Alpha-Amylase is the primary digestive enzyme acting on starch or glycogen, occurs in pancreas, parotid, serum, urine and occasionally in smaller amounts in other tissues or tumors, it has 496 amino acids [23]. X-ray diffraction technique was used to determine the structure of human pancreatic alpha-amylase. The active site residuesAsp 197, Glu 233, and Asp 300 were found to be located between Domains A and B. Further analysis revealed that substitution of either Glu233 or Asp300 side chains results in about 1000x decrease in catalytic activity. These findings were supported by the structural analysis of the Asp300Asn variant of human pancreatic alpha-amylase and its complex with acarbose which reflected its importance to the inhibitor binding mode [24,25].