EXPLORING THE POTENTIAL OF SHOUCHELLA OSHIMENSIS P-106 FOR CYCLODEXTRIN GLUCANOTRANSFERASE PRODUCTION

Cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) is an enzyme that utilizes starch by promoting an intramolecular transglycosylation reaction to produce cyclodextrins. An alkaliphilic, spore-forming, Gram-positive, potential CGTase producing bacteria was isolated from maize field and was identified as Shouchella oshimensis P-106 by 16S rDNA sequencing. The isolate P-106 efficiently produced 1.37 U/ml of β-CGTase as a major product and showed little existence of α- and γ-CGTase production. Optimization by one-factor-at-a-time (OFAT) approach significantly enhanced the β-CGTase production to 2.31 U/ml showed 1.68-fold increase.

Authors

Institutions

Publication Details

Journal
VIDYA - A JOURNAL OF GUJARAT UNIVERSITY
Published
2025-03-25
DOI
https://doi.org/10.47413/03szp371
Citations
1
Primary Topic
Enzyme Production and Characterization
Type
article
Field-Weighted Citation Impact
1.23
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

EXPLORING THE POTENTIAL OF SHOUCHELLA OSHIMENSIS P-106 FOR CYCLODEXTRIN GLUCANOTRANSFERASE PRODUCTION

Rushikesh Joshi, Rakeshkumar Ramanlal Panchal, Dimple S. Pardhi, Kiransinh Narendrasinh Rajput et al.
1 citations
VIDYA - A JOURNAL OF GUJARAT UNIVERSITY
Enzyme Production and Characterization
1.23
article

EXPLORING THE POTENTIAL OF SHOUCHELLA OSHIMENSIS P-106 FOR CYCLODEXTRIN GLUCANOTRANSFERASE PRODUCTION

Rushikesh Joshi, Rakeshkumar Ramanlal Panchal, Dimple S. Pardhi, Kiransinh Narendrasinh Rajput, Khushbu Rabadiya, Vikram H. Raval
article en
1 citations

Abstract

Cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) is an enzyme that utilizes starch by promoting an intramolecular transglycosylation reaction to produce cyclodextrins. An alkaliphilic, spore-forming, Gram-positive, potential CGTase producing bacteria was isolated from maize field and was identified as Shouchella oshimensis P-106 by 16S rDNA sequencing. The isolate P-106 efficiently produced 1.37 U/ml of β-CGTase as a major product and showed little existence of α- and γ-CGTase production. Optimization by one-factor-at-a-time (OFAT) approach significantly enhanced the β-CGTase production to 2.31 U/ml showed 1.68-fold increase.

VIDYA - A JOURNAL OF GUJARAT UNIVERSITYVol. 4(1)
Gujarat University (IN)
Openalex Percentile: Top 24%
Enzyme Production and Characterization
1.23
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.