Immobilization of α-amylases and Their Analytical Applications

Prakash, Om; Khare, Saumya

doi:10.1007/978-3-030-25023-2_6

Cited by 11 publications

(2 citation statements)

References 99 publications

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“…[37] Inhibitors of this enzyme can slow down carbohydrate absorption, prolonging total carbohydrate absorption time, decreasing the rate of glucose absorption, and subsequently reducing the postprandial plasma glucose increase. [38] The kingdoms of plants, animals, and microorganisms all include α-amylases. The majority of enzymes used in industrial operations come from microbial origins.…”

Section: α-Amylasementioning

confidence: 99%

“…From all these species, α‐amylase from microorganisms is preferred because of their plasticity for genetic manipulation and potential for economical bulk production [37] . Inhibitors of this enzyme can slow down carbohydrate absorption, prolonging total carbohydrate absorption time, decreasing the rate of glucose absorption, and subsequently reducing the postprandial plasma glucose increase [38] …”

Section: Introductionmentioning

confidence: 99%

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α‐Amylase Inhibitors Based on Thiazolidinone Skeleton: A Promising Approach in Diabetes Management

Singh,

Sindhu,

Kumar

et al. 2023

ChemistrySelect

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Thiazolidinone scaffold has become a promising scaffold when it comes to therapeutic importance, and researchers are quite interested in it because of its wide range of applications in the different fields of chemistry. The capacity of this nucleus to interact with a variety of biological targets, including the peroxisome proliferator‐activated receptor (PPAR), protein tyrosine phosphatase 1B, aldose reductase, α‐glucosidase, and α‐amylase, has led to the observation of its antidiabetic effect. α‐Amylase (α‐1,4‐glucan‐4‐glucanohydrolase, EC 3.2.1.1) is one of the most important industrial endoamylases capable of hydrolyzing the internal α‐1,4‐glycosidic bonds in polysaccharides with net retention of α‐anomeric configuration in low molecular weight products, such as glucose, maltose, and maltotriose units. The inhibitors of α‐amylase have the ability to lower endogenous activity, which is crucial for the management of agricultural pests as well as the treatment and prevention of human disorders. In the present review, we attempted to compile the most recent studies on thiazolidinone‐based α‐amylase inhibitors, investigate their therapeutic potential in treating diabetes, comprehend the relationships between structure and activity, offer suggestions for future research and translation of these findings into clinical applications. This comprehensive review strives to be a valuable resource for researchers, medicinal chemists, and healthcare professionals involved in developing and applying novel therapeutics for treating metabolic disorders.

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Section: α-Amylasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

α‐Amylase Inhibitors Based on Thiazolidinone Skeleton: A Promising Approach in Diabetes Management

Singh,

Sindhu,

Kumar

et al. 2023

ChemistrySelect

View full text Add to dashboard Cite

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Treatment of Starch Wastewater by α‐Amylase Immobilized on Silica Infused Magnetite Nanoparticles for Maltose Syrup Preparation

Patel,

Desai,

Patel

et al. 2023

Starch Stärke

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Casein decorated silicainfused magnetite (Fe3O4‐SiO2) nanoparticles are employed to immobilize commercial α‐amylase, where glutaraldehyde serves as a cross linker. The optimal concentration of variables, such as casein (1.4%w/v), Fe3O4‐SiO2 (106 µl), glutaraldehyde (55µl) and amylase (1 mg/ml) are defined by a Box Behnken design. The binding of casein, glutaraldehyde and enzyme over the nanoparticles are further confirmed structurally by fourier transform infrared spectroscopy (FTIR) and thermal gravimetric analysis (TGA). The loading capacity is 37 µg amylase over 1 µg of silica infused magnetite nanoparticles. The optimum pH for the catalysis of soluble and immobilized amylases is the same, i.e. pH 7. However, the pH range for catalysis is improved upon immobilization. The temperature optimum of soluble and immobilized amylases are 40 and 70 °C, respectively. The amylase stability is improved upon immobilization, as shown by enhanced half‐life and reduced deactivation rate constant. The immobilized amylase is used for 17 consecutive cycles with retention of 52% of the residual activity. The immobilized amylase produces high maltose syrup using the industrial wastewater containing corn starch. The ISO 5377 protocol determines dextrose equivalence values to be 36% and 24% during cycle 1 and cycle 2, respectively. The findings point out its possible commercial use.

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