Domain Structure and Function of α-1,3-Glucanase fromBacillus circulansKA-304, an Enzyme Essential for Degrading Basidiomycete Cell Walls

Suyotha, Wasana; Yano, Shigekazu; Takagi, Kazuyoshi; Rattanakit-Chandet, Nopakarn; Tachiki, Takashi; Wakayama, Mamoru

doi:10.1271/bbb.120900

Cited by 33 publications

(46 citation statements)

References 30 publications

(30 reference statements)

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“…The activity was determined according to the methods described previously (Suyotha et al, 2013). The reaction mixture containing 1% a-1,3-glucan, 50 mM citrate buffer (pH 5.5), and the appropriate amount of enzyme was incubated at 50∞C for 1 h. One unit of the enzyme was defined as the amount of enzyme releasing 1 mmol of reducing sugar (as glucose) per min.…”

Section: Methodsmentioning

confidence: 99%

“…a-1,3-Glucan was prepared with methods described previously (Suyotha et al, 2013). The other reagents were chemically pure grades of commercial products.…”

Section: Analysis Of N-terminal and Internal Amino Acid Sequencesmentioning

confidence: 99%

“…Key Words: a a a a a-1,3-glucanase; mycodextranase; Streptomyces thermodiastaticus; thermal stability 1,3-glucanase on degrading the cell wall of Schizophyllum commune (Suyotha et al, 2013(Suyotha et al, , 2014Yano et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…Another problem is the stability of the enzyme under the specific conditions conducted for oral care products, or a pesticide. Unfortunately, none of the characterized a-1,3-glucanases exhibit extreme stability, such as a high thermal stability, which is one of the properties desired for industrial utilization; almost all characterized a-1,3-glucanases were unstable above 65∞C (Fuglsang et al, 2000;Imai et al, 1977;Meyer and Phaff, 1980;Pleszczy¢ nska et al, 2010;Shimotsuura et al, 2008;Suyotha et al, 2013Suyotha et al, , 2014Tsumori et al, 2011). In recent years, genetic manipulations have been used to develop the properties of target enzymes.…”

Section: Introductionmentioning

confidence: 99%

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A novel thermostable α-1,3-glucanase from Streptomyces thermodiastaticus HF 3-3

Suyotha

Fujiki

Cherdvorapong

et al. 2017

J. Gen. Appl. Microbiol.

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Section: Methodsmentioning

confidence: 99%

“…a-1,3-Glucan was prepared with methods described previously (Suyotha et al, 2013). The other reagents were chemically pure grades of commercial products.…”

Section: Analysis Of N-terminal and Internal Amino Acid Sequencesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A novel thermostable α-1,3-glucanase from Streptomyces thermodiastaticus HF 3-3

Suyotha

Fujiki

Cherdvorapong

et al. 2017

J. Gen. Appl. Microbiol.

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“…Germinating conidia cultured in a 48-well plate were dropped onto a glass slide, washed twice with PBS, and fixed with 4% (w/v) paraformaldehyde for 10 min. Samples were washed twice with 50 mM potassium phosphate buffer (pH 6.5) and stained at room temperature for 2 h with Alexa Fluor 647–conjugated soybean agglutinin (SBA; 100 µg/mL) (Invitrogen) and α-1,3-glucanase-α-1,3-glucan–binding domain fused with GFP (AGBD-GFP; 100 µg/mL) (21) in 50 mM phosphate buffer (pH 6.5). After being washed with the same buffer, the samples were imaged under a FluoView FV1000 confocal laser-scanning microscope (Olympus, Tokyo, Japan).…”

Section: Methodsmentioning

confidence: 99%

Both galactosaminogalactan and α-1,3-glucan contribute to aggregation ofAspergillus oryzaehyphae in liquid culture

Miyazawa

Yoshimi

Sano

et al. 2019

Preprint

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226 words 2 Text, 5,353 words 3 3Abstract Filamentous fungi generally form aggregated hyphal pellets in liquid culture. 1 We previously reported that α-1,3-glucan-deficient mutants of Aspergillus nidulans did 2 not form hyphal pellets and their hyphae were fully dispersed, and we suggested that 3 α-1,3-glucan functions in hyphal aggregation. Yet, Aspergillus oryzae 4 α-1,3-glucan-deficient (AGΔ) mutants still form small pellets; therefore, we 5 hypothesized that another factor responsible for forming hyphal pellets remains in these 6 mutants. Here, we identified an extracellular matrix polysaccharide 7 galactosaminogalactan (GAG) as such a factor. To produce a double mutant of A. oryzae 8 (AG-GAGΔ), we disrupted the genes required for GAG biosynthesis in an AGΔ mutant. 9 Hyphae of the double mutant were fully dispersed in liquid culture, suggesting that 10 GAG is involved in hyphal aggregation in A. oryzae. Addition of partially purified GAG 11 fraction to the hyphae of the AG-GAGΔ strain resulted in formation of mycelial pellets. 12 Acetylation of the amino group in galactosamine of GAG weakened GAG aggregation, 13 suggesting that hydrogen bond formation by this group is important for aggregation. 14 Genome sequences suggest that α-1,3-glucan, GAG, or both are present in many 15 filamentous fungi and thus may function in hyphal aggregation in these fungi. We also 16 demonstrated that production of a recombinant polyesterase, CutL1, was higher in the 17 AG-GAGΔ strain than in the wild-type and AGΔ strains. Thus, controlling hyphal 18 aggregation factors of filamentous fungi may increase productivity in the fermentation 19 industry. 20 21 22Importance Production using filamentous fungi is an important part of the 1 fermentation industry, but hyphal aggregation in these fungi in liquid culture limits 2 productivity compared with that of yeast or bacterial cells. We found that 3 galactosaminogalactan and α-1,3-glucan both function in hyphal aggregation in 4 Aspergillus oryzae, and that the hyphae of a double mutant deficient in both 5 polysaccharides become fully dispersed in liquid culture. We also revealed the relative 6 contribution of α-1,3-glucan and galactosaminogalactan to hyphal aggregation. 7 Recombinant protein production was higher in the double mutant than in the wild-type 8 strain. Our research provides a potential technical innovation for the fermentation 9 industry that uses filamentous fungi, as regulation of the growth characteristics of A.10 oryzae in liquid culture may increase productivity. 11 12 13

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Synthesis and characterization of novel self-assembled amphiphilic α-1,3-glucan nanomicelles for drug delivery

Su,

Takeda,

Matsui

et al. 2023

Colloid Polym Sci

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Domain Structure and Function of α-1,3-Glucanase fromBacillus circulansKA-304, an Enzyme Essential for Degrading Basidiomycete Cell Walls

Cited by 33 publications

References 30 publications

A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

Both galactosaminogalactan and α-1,3-glucan contribute to aggregation ofAspergillus oryzaehyphae in liquid culture

Synthesis and characterization of novel self-assembled amphiphilic α-1,3-glucan nanomicelles for drug delivery

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