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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1948 1
1950 1
1953 1
1958 1
1959 1
1960 2
1962 2
1963 4
1964 1
1972 1
1974 1
1975 18
1976 26
1977 20
1978 16
1979 14
1980 10
1981 8
1982 23
1983 22
1984 26
1985 27
1986 22
1987 18
1988 17
1989 24
1990 19
1991 17
1992 6
1993 4
1994 7
1995 9
1996 6
1997 6
1998 9
1999 9
2000 6
2001 6
2002 6
2003 10
2004 7
2005 5
2006 10
2007 7
2008 5
2009 4
2010 7
2011 7
2012 9
2013 13
2014 6
2015 7
2016 7
2017 7
2018 5
2019 3
2020 0
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522 results
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Page 1
Fecal isoamylase activity in patients with pancreatic diseases.
Moriyoshi Y, et al. Pancreas 1991. PMID 1704633
The mean fecal amylase activity in healthy subjects was 757 +/- 88 IU/g (p-type isoamylase: 77 +/- 2%, s-type isoamylase: 23 +/- 2%). ...Daily fat intake did not affect fecal amylase or isoamylase activities. Fecal s-type isoamylase activity in patients with hypoacidity was significantly higher than in patients with hyperacidity, but no difference in fecal p-type isoamylase activity was observed. ...
The mean fecal amylase activity in healthy subjects was 757 +/- 88 IU/g (p-type isoamylase: 77 +/- 2%, s-type isoamylase: 23 + …
Engineering of isoamylase: improvement of protein stability and catalytic efficiency through semi-rational design.
Li Y, et al. J Ind Microbiol Biotechnol 2016. PMID 26597030
Isoamylase catalyzes the hydrolysis of α-1,6-glycosidic linkages in glycogen, amylopectin and α/β-limit dextrins. A semi-rational design strategy was performed to improve catalytic properties of isoamylase from Bacillus lentus. ...This work provides an effective strategy for improving the catalytic activity and stability of isoamylase, and the results obtained here may be useful for the improvement of catalytic properties of other α/β barrel enzymes....
Isoamylase catalyzes the hydrolysis of α-1,6-glycosidic linkages in glycogen, amylopectin and α/β-limit dextrins. A semi-rational des
Heterologous co-expression in E. coli of isoamylase genes from cassava Manihot esculenta Crantz 'KU50' achieves enzyme-active heteromeric complex formation.
Panpetch P, et al. Plant Mol Biol 2018. PMID 29380100
Cloning of two isoamylase genes, MeISA1 and MeISA2, from cassava (Manihot esculenta Crantz) tubers, accompanied by their co-expression in E. coli demonstrates a requirement for heteromeric complex formation to achieve debranching activity. Starch debranching enzyme (DBE) or isoamylase (ISA) (EC.3.2.1.68), an important enzyme in starch metabolism, catalyses the hydrolysis of α-1,6 glycosidic linkages of amylopectin. ...
Cloning of two isoamylase genes, MeISA1 and MeISA2, from cassava (Manihot esculenta Crantz) tubers, accompanied by their co-expressio …
The optimization of isoamylase processing conditions for the preparation of high-amylose ginkgo starch.
Hu L, et al. Int J Biol Macromol 2016. PMID 26780467
A high-amylose starch was prepared from ginkgo by hydrolysis using isoamylase and its structures (morphology and crystallinity) and physicochemical properties (swelling factor, water solubility and gelatinization) were determined. ...The present study has indicated that high-amylose starch prepared using isoamylase has unique functional properties, which lays the foundation for the wider application of ginkgo starch....
A high-amylose starch was prepared from ginkgo by hydrolysis using isoamylase and its structures (morphology and crystallinity) and p …
Enhanced Production of Recombinant Thermobifida fusca Isoamylase in Escherichia coli MDS42.
Ran H, et al. Appl Biochem Biotechnol 2016. PMID 27179515
To improve the yield of this important enzyme, the isoamylase from Thermobifida fusca was expressed in the reduced-genome E. coli strain MDS42. ...The greatest isoamylase activity (22,983.0 U/mL of culture) and production (18.8 mg/mL) were obtained 24 h after induction of expression. ...
To improve the yield of this important enzyme, the isoamylase from Thermobifida fusca was expressed in the reduced-genome E. coli str …
[Isoamylase].
Taniguchi H, et al. Tanpakushitsu Kakusan Koso 1985. PMID 4059576 Japanese.
Investigation of debranching pattern of a thermostable isoamylase and its application for the production of resistant starch.
Li Y, et al. Carbohydr Res 2017. PMID 28554014
In the present study, the action pattern of a thermostable isoamylase-type debranching enzyme on different types of starch was investigated. ...These data also help us better understand the application of isoamylase for preparation of other products from highly branched starch materials....
In the present study, the action pattern of a thermostable isoamylase-type debranching enzyme on different types of starch was invest …
Nucleotide sequence and expression of the isoamylase gene from an isoamylase-hyperproducing mutant, Pseudomonas amyloderamosa JD210.
Chen JH, et al. Biochim Biophys Acta 1990. PMID 2248978
The isoamylase gene (ISO) of Pseudomonas amyloderamosa JD210, an isoamylase-hyperproducing mutant, was cloned in an isoamylase-deficient and transformable mutant strain K31. ...In all transformed cells, the majority of the isoamylase produced was secreted and higher isoamylase activities were obtained in transformats with the transcriptional direction of the ISO gene similar to the nearby drug-determinant gene of the vector....
The isoamylase gene (ISO) of Pseudomonas amyloderamosa JD210, an isoamylase-hyperproducing mutant, was cloned in an isoamyl
Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice.
Fujita N, et al. Planta 1999. PMID 10333591
These results indicate that rice isoamylase possesses properties which are distinct from those reported for bacterial isoamylase. ...The nucleotide sequence and deduced amino acid sequence of the longest clone showed a high similarity to those of maize Surgary-1 isoamylase, but a lesser similarity to those of Pseudomonas amyloderamosa isoamylase. ...
These results indicate that rice isoamylase possesses properties which are distinct from those reported for bacterial isoamylase
Doubling Power Output of Starch Biobattery Treated by the Most Thermostable Isoamylase from an Archaeon Sulfolobus tokodaii.
Cheng K, et al. Sci Rep 2015. PMID 26289411 Free PMC article.
However, there is no thermostable isoamylase stable enough for simultaneous starch gelatinization and enzymatic hydrolysis, different from the case of thermostable alpha-amylase. ...This enzyme was the most stable isoamylase reported with a half lifetime of 200 min at 90 (o)C in the presence of 0.5 mM MgCl2, suitable for simultaneous starch gelatinization and isoamylase hydrolysis. ...
However, there is no thermostable isoamylase stable enough for simultaneous starch gelatinization and enzymatic hydrolysis, different …
522 results
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