Transglycosylation reaction of maltotriose-forming amylase from Streptomyces griseus
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry
Reference20 articles.
1. Direct spectrophotometric determination of alpha-amylase activity in salive, with p-nitrophenyl alpha-maltoside as substrate.
2. Mechanism of action of human pancreatic and salivary alpha-amylase on alpha-4-nitrophenyl maltoheptaoside substrate.
3. Differential Rate Assay of Human Pancreatic and Salivary α-Amylases in Serum Using Two Coupled Enzymes
4. Synthesis of p-nitrophenyl 65-O-benzyl-α-maltopentaoside, a substrate for alpha amylases
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1. Maltooligosaccharides: Properties, Production and Applications;Molecules;2023-04-06
2. Maltooligosaccharide-forming amylase: Characteristics, preparation, and application;Biotechnology Advances;2017-09
3. Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785;Applied Microbiology and Biotechnology;2015-01-27
4. Irradiation of Ultrasound onto Substrate Mixture Enhances Transglycosylating Activity of Commercial α-Amylase Preparation;Chemistry Letters;2005-10
5. Enzymatic synthesis of a new inhibitor of α-amylases: acarviosinyl-isomaltosyl-spiro-thiohydantoin;Carbohydrate Research;2005-05
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