Improved yields of cyclic nigerosylnigerose from starch by pretreatment with a thermostable branching enzyme

Aga, Hajime; Okamoto, Iwao; Taniguchi, Mituki; Kawashima, Akira; Abe, Hiroko; Chaen, Hiroto; Fukuda, Shigeharu

doi:10.1016/j.jbiosc.2009.09.047

Cited by 11 publications

(4 citation statements)

References 27 publications

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“…The specific activity of wild-type GBE was 299 ± 3 U/mg of protein when using amylose as the substrate. This was somewhat greater than the 63.75 U/mg obtained by Garg et al 20 and much greater than the 36 U/mg obtained by Aga et al 29 under similar conditions. When using amylopectin as the substrate, the M349T and M349S mutants showed 24.5% and 21.1% improvements in specific activity, respectively, compared with that of wild-type GBE.…”

Section: ■ Resultscontrasting

confidence: 53%

Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02

Liu

Ban

et al. 2017

J. Agric. Food Chem.

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1,4-α-Glucan branching enzyme (GBE, EC 2.4.1.18) is used to increase the number of α-1,6 branch points in starch and glycogen. On the basis of a multiple sequence alignment of the GBEs from a variety of bacteria, residue 349 (Geobacillus thermoglucosidans STB02 numbering) in region III is generally methionine in bacteria with higher identity, while it is threonine or serine in bacteria with lower identity. Four mutants (M349T, M349S, M349H, and M349Y) were constructed by site-directed mutagenesis and characterized. M349T and M349S showed 24.5% and 21.1% increases in specific activity compared with that of wild-type GBE, respectively. In addition, M349T and M349S displayed 24.2% and 17.6% enhancements in the α-1,6-glycosidic linkage ratio of potato starch samples, respectively. However, M349Y displayed a significant reduction in activity. Moreover, the mutations at M349 have a negligible effect on substrate specificity. Thus, M349T and M349S are more suitable for industrial applications than wild-type GBE.

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Section: ■ Resultscontrasting

confidence: 53%

Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02

Liu

Ban

et al. 2017

J. Agric. Food Chem.

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“…bl-GBE activity reached 80.88 U/mg for potato starch after renaturation. The specific activity of bl-GBE was 77.20 U/mg for amylose, which was higher than G. stearothermophilus (36 U/mg) (Aga et al 2010 ), Rhizomucor miehei (10.70 U/mg) (Wu et al 2014 ), and Mycobacterium tuberculosis (63.75U/mg) (Pal et al 2010b ). This showed that the higher catalytic efficiency of bl-GBE was conducive to its industrial applications.…”

Section: Discussionmentioning

confidence: 99%

Biochemical characteristics and potential application of a thermostable starch branching enzyme from Bacillus licheniformis

Yang

Liu

et al. 2023

AMB Expr

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Slowly digestible starch (SDS) has attracted increasing attention for its function of preventing metabolic diseases. Based on transglycosylation, starch branching enzymes (1,4-α-glucan branching enzymes, GBEs, EC 2.4.1.18) can be used to regulate the digestibility of starch. In this study, a GBE gene from Bacillus licheniformis (bl-GBE) was cloned, expressed, purified, and characterized. Sequence analysis and structural modeling showed that bl-GBE belong to the glycoside hydrolase 13 (GH13) family, with which its active site residues were conserved. The bl-GBE was highly active at 80 °C and a pH range of 7.5–9.0, and retained 90% of enzyme activity at 70 °C for 16 h. bl-GBE also showed high substrate specificity (80.88 U/mg) on potato starch. The stability and the changes of the secondary structure of bl-GBE at different temperature were determined by circular dichroism (CD) spectroscopy. The CD data showed a loss of 20% of the enzyme activity at high temperatures (80 °C), due to the decreased content of the α -helix in the secondary structure. Furthermore, potato starch treated with bl-GBE (300 U/g starch) showed remarkable increase in stability, solubility, and significant reduction viscosity. Meanwhile, the slowly digestible starch content of bl-GBE modified potato starch increased by 53.03% compared with native potato starch. Our results demonstrated the potential applications of thermophilic bl-GBE in food industries.

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“…Recent studies also found that when GBE was used in coordination with other amylases, the branching effect of mixed enzyme on starch was stronger than that of the single amylase. After the synergistic action of GBE and isoamylase on starch, the content of reducing sugar in the product obtained was remarkably higher than that in the product modified by a single enzyme [46]. In addition, Martinez et al found that the synergistic use of GBE and maltose amylase on starch can obtain modified starch with stronger anti-digestibility [47].…”

Section: Branching Structure Design Of Starch Moleculesmentioning

confidence: 99%

Engineering starch by enzymatic structure design for versatile applications in food industries: a critical review

Jiang²,

Kong³

et al. 2022

Syst Microbiol and Biomanuf

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As the second largest production material, starch has important value in textile, food, chemical and other fields. The shortcomings of natural starch can be solved, and its properties can be improved by modifying its structure, developing original properties, or introducing new functions, making it more suitable for certain application requirements. At present, the methods of starch modification mainly include chemical, physical, and enzymatic modification. In comparison with the two traditional modification methods (chemical and physical modification) mentioned above, enzymatic modification has the advantages of mild conditions, high substrate selectivity, and high product safety, and it is the most ideal green modification method. In this paper, we present an overview of the modified starch by enzymatic structure design. The modification process and mechanism for granule starch and gelatinized starch are summarized. Further, the difficulties encountered in starch modification by enzymatic modification were also analyzed. These analyses could pave a way for understanding and broadening the preparation and applications of modified starch, and provide theoretical references for the utilization of amylase in starch modification.

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Improved yields of cyclic nigerosylnigerose from starch by pretreatment with a thermostable branching enzyme

Cited by 11 publications

References 27 publications

Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02

Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02

Biochemical characteristics and potential application of a thermostable starch branching enzyme from Bacillus licheniformis

Engineering starch by enzymatic structure design for versatile applications in food industries: a critical review

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