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Aspects and recent trends in microbial α-amylase: a review
JS Paul, N Gupta, E Beliya, S Tiwari… - Applied Biochemistry and …, 2021 - Springer
Abstract α-Amylases are the oldest and versatile starch hydrolysing enzymes which can
replace chemical hydrolysis of starch in industries. It cleaves the α-(1, 4)-D-glucosidic …
replace chemical hydrolysis of starch in industries. It cleaves the α-(1, 4)-D-glucosidic …
Design of novel enzyme biocatalysts for industrial bioprocess: Harnessing the power of protein engineering, high throughput screening and synthetic biology
Biocatalysts have wider applications in various industries. Biocatalysts are generating
bigger attention among researchers due to their unique catalytic properties like activity …
bigger attention among researchers due to their unique catalytic properties like activity …
Bacterial and archaeal α-amylases: diversity and amelioration of the desirable characteristics for industrial applications
D Mehta, T Satyanarayana - Frontiers in Microbiology, 2016 - frontiersin.org
Industrial enzyme market has been projected to reach US $6.2 billion by 2020. Major
reasons for continuous rise in the global sales of microbial enzymes are because of …
reasons for continuous rise in the global sales of microbial enzymes are because of …
RETRACTED: Molecular improvements in microbial α-amylases for enhanced stability and catalytic efficiency
R Sindhu, P Binod, A Madhavan, US Beevi… - Bioresource …, 2017 - Elsevier
Abstract α-Amylases is one of the most important industrial enzyme which contributes to
25% of the industrial enzyme market. Though it is produced by plant, animals and microbial …
25% of the industrial enzyme market. Though it is produced by plant, animals and microbial …
Amylases from thermophilic bacteria: structure and function relationship
Amylases hydrolyze starch to diverse products including dextrins and progressively smaller
polymers of glucose units. Thermally stable amylases account for nearly 25% of the enzyme …
polymers of glucose units. Thermally stable amylases account for nearly 25% of the enzyme …
Native to designed: microbial α-amylases for industrial applications
Background α-amylases catalyze the endo-hydrolysis of α-1, 4-D-glycosidic bonds in starch
into smaller moieties. While industrial processes are usually performed at harsh conditions …
into smaller moieties. While industrial processes are usually performed at harsh conditions …
In vitro engineering of microbial enzymes with multifarious applications: prospects and perspectives
S Joshi, T Satyanarayana - Bioresource technology, 2015 - Elsevier
The discovery of a novel enzyme from a microbial source takes anywhere between months
to years, and therefore, there has been an immense interest in modifying the existing …
to years, and therefore, there has been an immense interest in modifying the existing …
α-Amylases
R Sindhu, P Binod, A Pandey - Current developments in biotechnology and …, 2017 - Elsevier
Amylases are among the most important enzymes used in industrial markets. α-Amylases
find specific application in various industrial processes such as starch liquefaction, desizing …
find specific application in various industrial processes such as starch liquefaction, desizing …
Molecular strategies to enhance stability and catalysis of extremophile-derived α-amylase using computational biology
N Gupta, E Beliya, JS Paul, S Tiwari, S Kunjam… - Extremophiles, 2021 - Springer
Abstract α-Amylase is the most significant glycoside hydrolase having applications in
various industries. It cleaves the α, 1–4 glucosidic linkages of polysaccharides like starch …
various industries. It cleaves the α, 1–4 glucosidic linkages of polysaccharides like starch …
Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger
Glucose oxidase (GOx) is a promising candidate for construction of implantable miniature
biofuel cells and biosensors for continuous glucose monitoring. The main drawback that …
biofuel cells and biosensors for continuous glucose monitoring. The main drawback that …