NDLI: A novel α-amylase from the cyanobacterium Nostoc sp. PCC 7119

Content Provider	Springer Nature Link
Author	Reyes Sosa, Francisco M. Molina Heredia, Fernando P. De la Rosa, Miguel A.
Copyright Year	2009
Abstract	Little information is yet available on the α-amylases of cyanobacteria. Here, the presence of an α-amylase in the cyanobacterium Nostoc sp. PCC 7119 is first demonstrated. A gene (amy1) encoding a cytoplasmic α-amylase (Amy1) protein has been identified, cloned, and overexpressed in Escherichia coli cells. The recombinant protein is a 56.7-kDa monomer, which has been purified to electrophoretic homogeneity by affinity chromatography. The substrate specificity and end product analyses confirm that it is a calcium-dependent α-amylase enzyme, which exhibits its maximum activity at 31°C and at pH between 6.5 and 7.5. The Amy1 protein breaks down mainly starch, is also able to cleave glycogen and dextrin, and exhibits no activity against xylan or pullulan. So the enzyme cannot efficiently attack the maltodextrins with degrees of polymerization below that of maltooctaose. Maltotriose, maltose, and maltotetraose are the major products of the enzymatic reaction with starch as substrate. The enzyme shows a very high turnover number against soluble potato starch (3,420 ± 270 s−1), as compared with other α-amylases reported in the literature. The high catalytic efficiency and relatively low optimum temperature of the Nostoc Amy1 protein make this previously unexplored group of cyanobacterial enzymes of great interest for further physiological studies and industrial applications.
Starting Page	131
Ending Page	141
Page Count	11
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	86
Issue Number	1
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-09-16
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Affinity chromatography α-amylase Cyanobacteria Endoglycosyl hydrolase Heterologous expression Nostoc Starch Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Molecular cloning and characterization of an α-amylase with raw starch digestibility fromBacillus sp. YX-1

Preferential and rapid degradation of raw rice starch by an α-amylase of glycoside hydrolase subfamily GH13_37

Cloning, heterologous expression, and comparative characterization of a mesophilic α-amylase gene from Bacillus subtilis JN16 in Escherichia coli

Characterization of hyperthermostable α-amylase from Geobacillus sp. IIPTN

Polyaniline-assisted silver nanoparticles: a novel support for the immobilization of α-amylase

Alcohol dehydrogenase AdhA plays a role in ethanol tolerance in model cyanobacterium Synechocystis sp. PCC 6803

Paenibacillus sp. 598K 6-α-glucosyltransferase is essential for cycloisomaltooligosaccharide synthesis from α-(1 → 4)-glucan

Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04

Improvement in lactic acid production from starch using α-amylase-secreting Lactococcus lactis cells adapted to maltose or starch

A novel α-amylase from the cyanobacterium Nostoc sp. PCC 7119

Similar Documents

Molecular cloning and characterization of an α-amylase with raw starch digestibility fromBacillus sp. YX-1

Preferential and rapid degradation of raw rice starch by an α-amylase of glycoside hydrolase subfamily GH13_37

Cloning, heterologous expression, and comparative characterization of a mesophilic α-amylase gene from Bacillus subtilis JN16 in Escherichia coli

Characterization of hyperthermostable α-amylase from Geobacillus sp. IIPTN

Polyaniline-assisted silver nanoparticles: a novel support for the immobilization of α-amylase

Alcohol dehydrogenase AdhA plays a role in ethanol tolerance in model cyanobacterium Synechocystis sp. PCC 6803

Paenibacillus sp. 598K 6-α-glucosyltransferase is essential for cycloisomaltooligosaccharide synthesis from α-(1 → 4)-glucan

Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04

Improvement in lactic acid production from starch using α-amylase-secreting Lactococcus lactis cells adapted to maltose or starch

A novel α-amylase from the cyanobacterium Nostoc sp. PCC 7119