Results 41 to 50 of about 804,350 (314)
Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase
Ecotoxicology and Environmental Safety, 2022 The digestive enzyme of plant are generally α-amylase. They functions enzyme that breakdown starch into maltose and sugars. This happens in the endosperm of the seed.
Ananthaselvam Azhagesan +2 more
doaj +1 more source
Microbial Cell Factories, 2011 Background Alkaline α-amylases have potential applications for hydrolyzing starch under high pH conditions in the starch and textile industries and as ingredients in detergents for automatic dishwashers and laundries.
Li Jianghua +4 more
doaj +1 more source
Cogent Food & Agriculture, 2016 α-amylase was produced by Aspergillus terreus NCFT 4269.10 using both liquid static surface (LSSF) and solid-state fermentation using pearl millet residues as substrate. The maximum production of α-amylase was noticed at 30°C incubated for 96h. The crude
Bijay Kumar Sethi +3 more
doaj +1 more source
Cloning and expression of an extracellular α-amylase gene fromStreptomyces hygroscopicusinStreptomyces lividans66 [PDF]
FEMS Microbiology Letters, 1986 An extracellular α-amylase gene was cloned from Streptomyces hygroscopicus into Streptomyces lividans 66 using the multicopy vector pIJ702. Subcloning of DNA from the original clone allowed the gene to be localized to a 2.8 kb segment of DNA. Use of a promoter probe vector gave a possible location of the gene promoter and also the direction of ...
Christine McKillop +2 more
openaire +1 more source
Porcine pancreatic α-amylase inhibitors from Euonymus laxiflorus Champ
, 2016 Twenty-six samples of indigenous medicinal plants were collected in Dak Lak Province of Vietnam and evaluated for α-amylase inhibitory activity. Of these samples, trunk bark extract from Euonymus laxiflorus Champ.
Quang Vinh Nguyen +4 more
core +1 more source
Effect of ultrasonic treatment on enzyme activity of liquid α-amylase
, 2023 The enzyme activity of liquid α-amylase treated by ultrasonic is discussed by using iodine and starch chromatometry. The effects of ultrasonic power, ultrasonic time, pH value of enzyme solution, standing time by ultrasonic treatment, temperature on ...
C H Yi (13367517) +4 more
core
Changes in the cell envelope structure ofClostridiumsp. strain EM1 during massive production of α-amylase and pullulanase [PDF]
FEMS Microbiology Letters, 1987 Marked changes in cell envelope structure were observed when Clostridium sp. strain EM1 cells grown in continuous culture under glucose limitation were compared with cells grown under starch limitation. The increase in the level of extracellular α-amylase and pullulanase during starch-limited growth was parallelled by degradation of the cell-envelope ...
G. Antranikian +3 more
openaire +1 more source
Cloning and expression of the thermostable α-amylase gene fromClostridium thermosulfurogenes(DSM 3896) inEscherichia coli [PDF]
FEMS Microbiology Letters, 1989 The gene coding for a thermostable α-amylase from Clostridium thermosulfurogenes (DSM 3896) was cloned in Escherichia coli using pUC18 as a vector. The recombinant plasmid pCT2 of an amylolytic positive transformant of E. coli contained a 2.9 kbp fragment of chromosomal DNA of C. thermosulforogenes carrying the α-amylase gene. In E.
K. Haeckel, H. Bahl
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Bread Spoilage Fungi as Creators of α Amylase Using Two Types of Wheat Flour
BioResources, 2023 Fungal spoilage of bread can be a great problem; however, it can be explored as a producer of enzymes. The fungi were isolated from breads, and their activity for α-amylase production was planned.
Aisha M. H. Al-Rajhi +4 more
doaj +2 more sources
Construction of α-amylase-producing strains not subject to carbon catabolite repression [PDF]
FEMS Microbiology Letters, 2002 The dyatic symmetric element (DSE) present in the alpha-amylase gene promoter region of the thermophilic Streptomyces strain sp. TO1, and the whole alpha-amylase gene (amy TO1) with a 3-bp change in the DSE, were cloned in the high copy number replicative cloning vector pIJ702 giving pLM10 and pLM11 plasmids respectively.
Lotfi, Mellouli +2 more
openaire +2 more sources