Siting Feng
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Siting Feng has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Fei Wang
College of Bioscience and Bioengineering, Jiangxi Agricultural University, Nanchang 330045, China
1 shared publication - Guorong Ni
College of Land Resources and Environment, Jiangxi Agricultural University, Nanchang 330045, China
1 shared publication - Jialei Wu
College of Bioscience and Bioengineering, Jiangxi Agricultural University, Nanchang 330045, China
1 shared publication - Jun Liu
College of Bioscience and Bioengineering, Jiangxi Agricultural University, Nanchang 330045, China
1 shared publication - Weiqi Zhang
College of Bioscience and Bioengineering, Jiangxi Agricultural University, Nanchang 330045, China
1 shared publication - Yusen Hu
College of Bioscience and Bioengineering, Jiangxi Agricultural University, Nanchang 330045, China
1 shared publication
Latest Publications
- Open Access
Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) from Myxococcus sp. Strain V11
A novel multifunctional isoamylase, MIsA from Myxococcus sp. strain V11, was expressed in Escherichia coli BL21(DE3). Sequence alignment revealed that MIsA is a typical isoamylase that belongs to glycoside hydrolase family 13 (GH 13). MIsA can hydrolyze the α-1,6-branches of amylopectin and pullulan, as well as the α-1,4-glucosidic bond in amylose. Additionally, MIsA demonstrates 4-α-D-glucan transferase activity, enabling the transfer of α-1,4-glucan oligosaccharides between molecules, particularly with linear maltooligosaccharides. The Km, Kcat, and Vmax values of the MIsA for amylopectin were 1.22 mM, 40.42 µmol·min–1·mg–1, and 4046.31 mM·min–1. The yields of amylopectin and amylose hydrolyzed into oligosaccharides were 10.16% and 11.70%, respectively. The hydrolysis efficiencies were 55%, 35%, and 30% for amylopectin, soluble starch, and amylose, respectively. In the composite enzyme hydrolysis of amylose, the yield of maltotetraose increased by 1.81-fold and 2.73-fold compared with that of MIsA and MTHase (MCK8499120) alone, respectively.
Open AccessMolecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) from Myxococcus sp. Strain V11
A novel multifunctional isoamylase, MIsA from Myxococcus sp. strain V11, was expressed in Escherichia coli BL21(DE3). Sequence alignment revealed that MIsA is a typical isoamylase that belongs to glycoside hydrolase family 13 (GH 13). MIsA can hydrolyze the α-1,6-branches of amylopectin and pullulan, as well as the α-1,4-glucosidic bond in amylose. Additionally, MIsA demonstrates 4-α-D-glucan transferase activity, enabling the transfer of α-1,4-glucan oligosaccharides between molecules, particularly with linear maltooligosaccharides. The Km, Kcat, and Vmax values of the MIsA for amylopectin were 1.22 mM, 40.42 µmol·min–1·mg–1, and 4046.31 mM·min–1. The yields of amylopectin and amylose hydrolyzed into oligosaccharides were 10.16% and 11.70%, respectively. The hydrolysis efficiencies were 55%, 35%, and 30% for amylopectin, soluble starch, and amylose, respectively. In the composite enzyme hydrolysis of amylose, the yield of maltotetraose increased by 1.81-fold and 2.73-fold compared with that of MIsA and MTHase (MCK8499120) alone, respectively.