Asset Details
Do you wish to reserve the book?
Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785
Do you wish to request the book?
Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785
2015
Overview
A maltotriose-forming amylase (G3Amy) from Kitasatospora sp. MK-1785 was successfully isolated from a soil sample by inhibiting typical extracellular α-amylases using a proteinaceous α-amylase inhibitor. G3Amy was purified from the MK-1785 culture supernatant and characterized. G3Amy produced maltotriose as the principal product from starch and was categorized as an exo-α-amylase. G3Amy could also transfer maltotriose to phenolic and alcoholic compounds. Therefore, G3Amy can be useful for not only maltotriose manufacture but also maltooligosaccharide-glycoside synthesis. Further, the G3Amy gene was cloned and expressed in Escherichia coli cells. Analysis of its deduced amino acid sequence revealed that G3Amy consisted of an N-terminal GH13 catalytic domain and two C-terminal repeat starch-binding domains belonging to CBM20. It is suggested that natural G3Amy was subjected to proteolysis at N-terminal region of the anterior CBM20 in the C-terminal region. As with natural G3Amy, recombinant G3Amy could produce and transfer maltotriose from starch.
Publisher
Springer-Verlag,Springer Berlin Heidelberg,Springer,Springer Nature B.V
Subject
/ Amylases
/ Biomedical and Life Sciences
/ Biotechnologically Relevant Enzymes and Proteins
/ Cloning
/ E coli
/ Enzymes
/ Escherichia coli - enzymology
/ genes
/ Microbial Genetics and Genomics
/ Phenols
/ Proteins
/ RNA, Ribosomal, 16S - genetics
/ soil
/ Starch
/ Streptomycetaceae - classification
/ Streptomycetaceae - enzymology
/ Streptomycetaceae - genetics
/ Streptomycetaceae - isolation & purification
/ Studies
