Evaluation of α-Amylase Inhibitory Activity of Aqueous Extracts of Selected Plants | Chapter 2 | Pharmaceutical Science: New Insights and Developments Vol. 10

 

Background: Diabetes is a chronic, metabolic disease characterised by elevated levels of blood glucose (or blood sugar), leading to serious damage to the heart, blood vessels, eyes, kidneys and nerves. Naturally occurring inhibitors of carbohydrate-digesting enzymes may offer an effective way to limit the absorption of dietary carbohydrates while causing fewer adverse effects than synthetic drugs. α-amylase helps in the digestion and absorption of dietary starch and causes elevated blood glucose levels.

 

Aims: The present work aims to find natural α-amylase inhibitors derived from plants that have gained popularity as safe and cost-effective alternatives.

 

Study Design: This study investigates the α-amylase inhibitory potential of five medicinal plants (Aerva lanata, Emblica officinalis, Momordica charantia, Musa paradisiaca, and Psidium guajava) traditionally used in diabetes management.

 

Place and Duration of Study: The study was conducted at the Department of Botany, Catholicate College, Pathanamthitta, Kerala, India.

 

Methodology: The α-amylase inhibitory activity of five plant extracts (Aerva lanata, Emblica officinalis, Momordica charantia, Musa paradisiaca, and Psidium guajava) was evaluated at concentrations ranging from 10, 20, 40, 60, 80 and 100 μg/mL. Metformin was used as a standard antidiabetic drug for comparison. The extracts underwent additional phytochemical analysis to determine their total tannin and total phenolic contents.

 

Results: Our findings demonstrate that these plant extracts exhibit varying degrees of α-amylase inhibitory activity, with Momordica charantia showing the highest inhibition (95.00% ± 0.58% at 100 μg/mL). The inhibitory potential of these extracts correlates with their phenolic and tannin content, suggesting a role for these phytochemicals in α-amylase inhibition. Notably, Emblica officinalis and Psidium guajava also displayed significant inhibitory activity comparable to the standard drug metformin.

 

Conclusion: The study provides valuable insights into the development of novel antidiabetic therapies from natural sources. Further studies are warranted to isolate and characterise the bioactive compounds and elucidate their mechanisms of action. The findings of this study have significant implications for the management of diabetes and the development of natural antidiabetic agents.

 

 

Author(s) Details

Nisha Joseph
Post Graduate and Research Department of Botany, Catholicate College Pathanamthitta, Kerala, India.

 

A. S. Deepthi
Post Graduate and Research Department of Botany, Catholicate College Pathanamthitta, Kerala, India.

 

Gokul G. Nair
Post Graduate and Research Department of Botany, Catholicate College Pathanamthitta, Kerala, India.

 

Merin Grace Jiji
Post Graduate and Research Department of Botany, Catholicate College Pathanamthitta, Kerala, India.

 

Please see the book here :- https://doi.org/10.9734/bpi/psnid/v10/7036

Exploring the Potential of α-Amylase: Genetic Identification, Purification Techniques and Its Applications | Chapter 7 | Contemporary Research and Perspectives in Biological Science Vol. 5

α-Amylase is a key enzyme widely employed in various industrial applications, including foodstuffs, fabric goods, and biofuel production. In our review study, we focused on genetically characterized microbial isolates that produce α-amylase from diverse sources. DNA isolation was performed using an alkaline lysis protocol followed by PCR amplification of the 16S rRNA gene. After isolating DNA samples, the 16S rRNA gene was PCR-amplified, and the phylogenetic relationships were determined through sequencing and subsequent analysis. To optimize enzyme production, various parameters such as pH, temperature, and incubation time were investigated. To purify the α-amylase enzyme, several purification techniques were employed. The crude amylase enzyme preparation was precipitated using ammonium sulfate. After dialysis and size exclusion chromatography, the purified enzyme preparation was analyzed further. To assess purity, the dialyzed samples were analyzed using a suitable chromatographic method to separate and evaluate the sample components. α-amylase characterization involved molecular weight determination by using SDS-PAGE, size determination by Size exclusion chromatography, and comprehensive examination was done by using mass spectrometry. In conclusion, this study successfully compared the genetically identified and characterized α-amylase producing microbial isolates. The optimized incubation conditions and purification techniques provided valuable insights into the production and purification of this industrially important enzyme. α-Amylase enzymes play an essential role in several industrial processes, improving and facilitating eco-friendly methods in areas such as textile, food, pharmaceutical, and alcohol manufacturing. Their adaptability drives cross-sector, sustainable innovations.

Further studies can focus on enhancing the enzyme's characteristics and exploring its potential applications in various industries.

 

Author (s) Details

 

Arvind Sharma
Department of Zoology, B.K.S.N. Govt. College Shajapur (M.P.), India.

 

R.K. Sharma
Department of Botany, B.K.S.N. Govt. College Shajapur (M.P.), India.

 

Please see the book here:- https://doi.org/10.9734/bpi/crpbs/v5/2929

Phytochemical Analysis by HR-LCMS and In-vitro Anti - diabetic Potential of Michelia champaca Bark| Chapter 3 | Novel Aspects on Pharmaceutical Research Vol. 4

 The current study was proposed to explore the basic phytochemicals and HRLCMS was performed to separate and sequester the phytoconstituents present in Michelia champaca established on their memory time. Natural amount are organic fragments with a type of structural features and biological exercises that have evolved by way of long-term evolutionary theory and evolution. They are more reliable and more affordable than artificial products. The plant example for the proposed report was increased from Tirupati District of Andhra Pradesh in the month of February 2018. The consequences of HR-LCMS showed the vicinity of 15 phytochemical compounds. DL-Carnitine, Catechin, D-α-Tocopherol, Colchicine, Myricetin, Epicatechin, Quercetin, Epigallocatechin gallate, Quercetin-3β-D-glucoside, Kaempferol, Sorbic acid, Apocynin, Epigallocatechin gallate, myricetin 3-O-beta-D-galactopyranoside, Naringeninchalcone are the main compounds labeled. In the experimental models, the hindrance of enzymes such as -amylase and -glucosidase delays the rate of sweet liquid absorption and lowers level of glucose in blood levels. In HR-LCMS elucidation, the compounds like DL-Carnitine, Catechin, D-α-Tocopherol, Colchicine, Myricetin, Epicatechin, Quercetin, Epigallocatechin gallate, Quercetin-3β-D-glucoside, Kaempferol, Sorbic acid, Apocynin, Ellagic acid, myricetin 3-O-being tested-D-galactopyranoside, Naringeninchalcone were present in Michelia champaca (Bark). The IC50 values of α-amylase and α-glucosidase inhibitory exercise of HEMC was acquired expected 88.65 μg/mL and 71.28 μg/mL correspondingly. Positive control acarbose presented IC50 value of 52.94 μg/mL and 50.01 μg/mL similarly. The present data hinted that the extracts possess direct and forceful antioxidant activities through diversified mechanisms.

Author(s) Details:

Segu Prathyusha,
Department of Pharmacognosy, School of Pharmacy, Guru Nanak Institutions Technical Campus (Autonomous), Hyderabad – 501506, Telangana, India and Department of Pharmacognosy, Vels Institute of Science, Technology and Advanced Studies, Chennai – 600117, Tamil Nadu, India.

Malarkodi Velraj,
Department of Pharmacognosy, Vels Institute of Science, Technology and Advanced Studies, Chennai – 600117, Tamil Nadu, India.

Please see the link here: https://stm.bookpi.org/NAPR-V4/article/view/11001

Determining the Pancreatic Arginase Activity and α- Amylase Levels in Patients with Type 2 Diabetes and Alcoholic Pancreatitis | Chapter 2 | Challenging Issues on Environment and Earth Science Vol. 5

 Arginase, a regenerative enzyme found in the endocrine pancreas, participates in insulin metabolism as well as regenerative processes during polyamine formation. High levels of -amylase have been linked to pancreatic damage. The purpose of this study was to see how arginase and -amylase functioned in the pancreas of people with type 2 diabetes and those who had alcohol-induced acute pancreatitis. Arginase and -amylase activities in pancreatic tissue were measured in patients with type 2 diabetes mellitus or acute pancreatitis without pancreatic diabetes. The results were compared to those of a control group. Our findings show that diabetic pancreas has higher arginase activity than controls, whereas pancreatitis tissues have lower arginase activity (P 0.05). The activity of a-amylase was higher in the pancreas of type 2 diabetes patients than in the pancreas of acute pancreatitis patients. Rather than being a source of damage mediators, increased arginase activity in type 2 diabetes patients may be associated with an effort to reclaim endocrine pancreatic function. Because pancreatitis causes acinar damage, resulting in the release of a-amylase, this enzyme was found to be higher in diabetic pancreatic tissue than in nondiabetic pancreatic tissue.

Author (S) Details

José D. Méndez
Medical Research Unit in Metabolic Diseases, Cardiology Hospital, National Medical Center, Mexican Institute of Social Security, México.

Roberto De Haro
Medicine Section, Iztacala Faculty, National Autonomous University of Mexico, Los Reyes Iztacala, Tlalnepantla, State of Mexico, 54090, Mexico.

Verna Méndez-Valenzuela
General Hospital 49, Mexican Institute of Social Security, Los Moch, México.

Jorge L. Ble-Castillo
Research Station in DACS. Juárez Autonomous University of Tabasco, Avenida Gregorio Méndez 2890 Colonia Tamulte. 86100. Villahermosa, Tabasco, Mexico.

Hector O. Rubio
Faculty of Zootechnology and Ecology, Autonomous University of Chihuahua, Periferico Francisco R. Almada, Km 1, CP: 31453. Chihuahua, México.

View  Book :-  https://stm.bookpi.org/CIEES-V5/article/view/1826