Gene cloning, functional expression and characterisation of a novel glycogen branching enzyme from Rhizomucor miehei and its application in wheat breadmaking

Wu, Shupeng; Liu, Yu; Yan, Qiaojuan; Jiang, Zhengqiang

doi:10.1016/j.foodchem.2014.02.161

Cited by 29 publications

(25 citation statements)

References 37 publications

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“…Rhizomucor miehei (Wu et al 2014). The results of substrate specificities show that PsGBE prefers amylose rather than highlybranched amylopectin.…”

Section: Substrate Specificity Of Psgbe the Substrate Specificity Ofmentioning

confidence: 94%

“…GBEs losing more than 50% activity below 30℃ (Kiel et al 1989, Lim et al 2003, PsGBE exhibited more than 80% activity in the low temperature range of 15 _ 30℃, which may have potential use in the food industry like the glycogen branching enzyme RmGBE from Rhizomucor miehei (Wu et al 2014). …”

Section: Biochemical Properties Of Psgbementioning

confidence: 99%

“…So, high concentrations of PsGBE could increase the specific volume of bread. Fungal glycogen branching enzyme also could increase the specific volume of bread (Wu et al 2014). BSuA, an effective antifirming α-amylase widely used in breadmaking, could increase the bread volume only to 6.72% (Goesaert et al 2009).…”

Section: Effects Of Psgbe On Bread Qualitymentioning

confidence: 99%

“…The GBEs have been identified and biochemically characterized from Cyanobacterium synechococcus (Kiel et al 1989), Neurospora crassa (Kawabata et al 2002), Rhizomucor miehei (Wu et al 2014), Bacillus stearothermophilus (Takata et al 1994), Neisseria denitrificans (Büttcher et al 1999), Streptococcus mutans (Kim et al 2008) and Rhodothermus obamensis (Roussel et al 2013), but only few of them have been purified and characterized. Most of GBEs display maximal activity within the mesophilic temperature range and neutral pH (Kiel et al 1989, Lee et al 2010, Thiemann et al 2006.…”

Section: Introductionmentioning

confidence: 99%

“…GBEs can specifically catalyze the α-1, 4-glycosidic linkages of starch, changing its structure and decreasing amylose percentage in starch, to reduce the retrogradation. Starch modified by GBEs is applied to improve the quality of food products, such as cookies, cakes and breads (Spendler et al 1997, Wu et al 2014, Oliveira et al 2014. GBE from N. crassa can increase the solubility and stability of starch solutions (Kawabata et al 2002).…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Purification and Characterization of a Novel Glycogen Branching Enzyme from <i>Paenibacillus</i> sp. SSG-1 and its Application in Wheat Bread Making

Cao

et al. 2016

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“…Rhizomucor miehei (Wu et al 2014). The results of substrate specificities show that PsGBE prefers amylose rather than highlybranched amylopectin.…”

Section: Substrate Specificity Of Psgbe the Substrate Specificity Ofmentioning

confidence: 94%

Section: Biochemical Properties Of Psgbementioning

confidence: 99%

Section: Effects Of Psgbe On Bread Qualitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Purification and Characterization of a Novel Glycogen Branching Enzyme from <i>Paenibacillus</i> sp. SSG-1 and its Application in Wheat Bread Making

Cao

et al. 2016

FSTR

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Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes

2021

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Glycoside hydrolase family 57 glycogen branching enzymes (GH57GBE) catalyze the formation of an α‐1,6 glycosidic bond between α‐1,4 linked glucooliogosaccharides. As an atypical family, a limited number of GH57GBEs have been biochemically characterized so far. This study aimed at acquiring a better understanding of the GH57GBE family by a systematic sequence‐based bioinformatics analysis of almost 2500 gene sequences and determining the branching activity of several native and mutant GH57GBEs. A correlation was found in a very low or even no branching activity with the absence of a flexible loop, a tyrosine at the loop tip, and two β‐strands.

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A glycogen branching enzyme from Thermomonospora curvata: Characterization and its action on maize starch

et al. 2015

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A gene (TcGBE) encoding a glycogen branching enzyme from Thermomonospora curvata was expressed in Escherichia coli and purified, and biochemically analyzed. The purified enzyme was approximately 84 kDa, and exhibited a maximum activity at 55°C and pH 8.5. The enzyme showed the highest specificity to amylose with a specific activity of 90.28 U/mg. The recombinant enzyme could act on maize starch, and starch treated with TcGBE was observed to have a lower amylose content and molecular weight. The number of short chains of amylopectin in TcGBEmodified starch with a degree of polymerization (DP) less than 13 increased from 20.19 to 32.59%, and was accompanied by a reduction in longer chains (DP > 25) from 25.58 to 10.03%. In addition, the medium length chains of amylopectin (13 < DP <25) also showed a slight increase from 54.23 to 58.38%. The 1 H NMR spectra revealed an increased ratio of a-1,6-to a-1, 4-glucosidic linkages from 4.1 to 10.3% following treatment with TcGBE for 10 h. Taken together, these results suggested that TcGBE could be used to generate a modified maize starch with a low amylose content and more branched amylopectin of low molecular weight but richer in short and intermediate chains.

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Gene cloning, functional expression and characterisation of a novel glycogen branching enzyme from Rhizomucor miehei and its application in wheat breadmaking

Cited by 29 publications

References 37 publications

Purification and Characterization of a Novel Glycogen Branching Enzyme from <i>Paenibacillus</i> sp. SSG-1 and its Application in Wheat Bread Making

Purification and Characterization of a Novel Glycogen Branching Enzyme from <i>Paenibacillus</i> sp. SSG-1 and its Application in Wheat Bread Making

Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes

A glycogen branching enzyme from Thermomonospora curvata: Characterization and its action on maize starch

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