Senescence of the Lentinula edodes Fruiting Body After Harvesting

Sakamoto, Yuichi; Nakade, Keiko; Konno, Naotake; Sato, Toshitsugu

doi:10.5772/33675

Cited by 37 publications

(20 citation statements)

References 112 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4b). Thus, II-3 was apparently an exo-1,3-b-glucanase (EXG) (Pitson et al, 1993;Sakamoto et al, 2012) rather than a 1,3-b-glucosidase. Furthermore, TLC analysis showed that EXG did not exhibit appearance of any laminarioligosaccharides with higher degrees of polymerization than the substrates; thus, II-3 must lack transglycosylation activity toward laminarioligosaccharides (Fig.…”

Section: Substrate Specificity and Mode Of Actionmentioning

confidence: 99%

“…The cell wall of the fruiting body is constructed mainly of chitin and 1,3-b-glucan with 1,6-b-linked branches (Kamada et al, 1991;Sakamoto et al, 2012). During the development of fruiting bodies, basidiomycetes produce some hydrolytic enzymes associated with these polysaccharides in cell walls.…”

Section: Introductionmentioning

confidence: 99%

“…During the development of fruiting bodies, basidiomycetes produce some hydrolytic enzymes associated with these polysaccharides in cell walls. These fungal glycoside hydrolases act on cell wall components and are considered to be responsible for cell wall extension (Kamada et al, 1991;Lim & Choi, 2009;Muraguchi et al, 2008;Tao et al, 2013), cell wall remodelling (Bowman & Free, 2006;Cabib & Arroyo, 2013;Gastebois et al, 2009;Mouyna et al, 2013) and fruiting body autolysis (Fukuda et al, 2008;Kües, 2000;Minato et al, 2004;Sakamoto et al, 2012;Tao et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…Two endo-1,3-bglucanases, TLG1 and GLU1, and one exo-1,3-b-glucanase, EXG2, were suggested to be involved in lentinan degradation after harvesting (Sakamoto et al, 2006(Sakamoto et al, , 2011(Sakamoto et al, , 2012. L. edodes GLU1 and TLG1 belong to a glyco_hydro_128 family and a thaumatin-like protein, respectively, rather than a glyco_hy-dro_16 family, so perhaps different basidiomycete species utilize different types of endo-1,3-b-glucanases to degrade 1,3-b-glucan in their cell walls.…”

mentioning

confidence: 99%

“…L. edodes GLU1 and TLG1 belong to a glyco_hydro_128 family and a thaumatin-like protein, respectively, rather than a glyco_hy-dro_16 family, so perhaps different basidiomycete species utilize different types of endo-1,3-b-glucanases to degrade 1,3-b-glucan in their cell walls. L. edodes EXG2 has 65 % identity with C. cinerea EXG; it degraded 1,3/1,6-b-glucan (lentinan) to produce glucose, laminaribiose, gentiobiose and some other oligosaccharides (Sakamoto et al, 2005b(Sakamoto et al, , 2012, rather than only glucose and gentiobiose as the C. cinerea EXG did. It is notable that in those studies the combined action of GLU1 and EXG2 from L. edodes on 1,3-b-glucan produced glucose and disaccharides (laminaribiose) as end products; however, how the laminaribiose was further degraded to a single glucose was not addressed (Sakamoto et al, 2012).…”

mentioning

confidence: 99%

See 4 more Smart Citations

Purification, characterization and synergism in autolysis of a group of 1,3-β-glucan hydrolases from the pilei of Coprinopsis cinerea fruiting bodies

et al. 2015

View full text Add to dashboard Cite

Using a combined chromatography method, we simultaneously purified three protein fractions (II-2, II-3 and II-4) with 1,3-b-glucanase activity from extraction of pilei of Coprinopsis cinerea fruiting bodies. MALDI-TOF/TOF amino acid sequencing showed that these three fractions matched a putative exo-1,3-b-glucanase, a putative glucan 1,3-b-glucosidase and a putative glycosyl hydrolase family 16 protein annotated in the C. cinerea genome, respectively; however, they were characterized as a 1,3-b-glucosidase, an exo-1,3-b-glucanase and an endo-1, 3-b-glucanase, respectively, by analysis of their substrate specificities and modes of action. This study explored how these three 1,3-b-glucoside hydrolases synergistically acted on laminarin: the endo-1,3-b-glucanase hydrolysed internal glycosidic bonds of laminarin to generate 1,3-b-oligosaccharides of various lengths, the exo-1,3-b-glucanase cleaved the longer-chain laminarioligosaccharides into short-chain disaccharides, laminaribiose and gentiobiose, and the 1,3-b-glucosidase further hydrolysed laminaribiose to glucose. The remaining gentiobiose must be hydrolysed by other 1,6-b-glucosidases. Therefore, the endo-1,3-b-glucanase, exo-1,3-b-glucanase and 1,3-b-glucosidase may act synergistically to completely degrade the 1,3-b-glucan backbone of the C. cinerea cell wall during fruiting body autolysis. These three 1,3-b-glucoside hydrolases share a similar optimum pH and optimum temperature, supporting the speculation that these enzymes work together under the same conditions to degrade 1,3-b-glucan in the C. cinerea cell wall during fruiting body autolysis.

show abstract

Section: Substrate Specificity and Mode Of Actionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Purification, characterization and synergism in autolysis of a group of 1,3-β-glucan hydrolases from the pilei of Coprinopsis cinerea fruiting bodies

et al. 2015

View full text Add to dashboard Cite

show abstract

TMT‐MS/MS proteomic analysis of the carbohydrate‐active enzymes in the fruiting body of Pleurotus tuoliensis during storage

Zou

Zheng

et al. 2020

J Sci Food Agric

View full text Add to dashboard Cite

BACKGROUND The fruiting body of Pleurotus tuoliensis deteriorates rapidly after harvest, causing a decline in its commercial value and a great reduction in its shelf life. According to the present research, carbohydrate‐active enzymes (CAZymes) may cause the softening, liquefaction and autolysis of mature mushrooms after harvest. To further understand the in vivo molecular mechanism of CAZymes affecting the postharvest quality of P. tuoliensis fruiting bodies, a tandem mass tags labelling combined liquid chromatography–tandem mass spectrometry (TMT‐MS/MS) proteomic analysis was performed on P. tuoliensis fruiting bodies during storage at 25 °C. RESULTS A total of 4737 proteins were identified, which had at least one unique peptide and had a confidence level above 95%. Consequently, 1307 differentially expressed proteins (DEPs) were recruited using the criteria of abundance fold change (FC) >1.5 or < 0.67 and P < 0.05. The identified proteins were annotated by dbCAN2, a meta server for automated CAZymes annotation. Subsequently, 222 CAZymes were obtained. Several CAZymes participating in the cell wall degradation process, including β‐glucosidase, glucan 1,3‐β‐glucosidase, endo‐1,3(4)‐β‐glucanase and chitinases, were significantly upregulated during storage. The protein expression level of CAZymes, such as xylanase, amylase and glucoamylase, were upregulated significantly, which may participate in the P. tuoliensis polysaccharide degradation. CONCLUSIONS The identified CAZymes degraded the polysaccharides and lignin, destroying the cell wall structure, preventing cell wall remodeling, causing a loss of nutrients and the browning phenomenon, accelerating the deterioration of P. tuoliensis fruiting body. © 2020 Society of Chemical Industry

show abstract

De novo transcriptome and proteome analysis of Dictyophora indusiata fruiting bodies provides insights into the changes during morphological development

Wang

Wen

Yang

et al. 2020

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Senescence of the Lentinula edodes Fruiting Body After Harvesting

Cited by 37 publications

References 112 publications

Purification, characterization and synergism in autolysis of a group of 1,3-β-glucan hydrolases from the pilei of Coprinopsis cinerea fruiting bodies

Purification, characterization and synergism in autolysis of a group of 1,3-β-glucan hydrolases from the pilei of Coprinopsis cinerea fruiting bodies

TMT‐MS/MS proteomic analysis of the carbohydrate‐active enzymes in the fruiting body of Pleurotus tuoliensis during storage

De novo transcriptome and proteome analysis of Dictyophora indusiata fruiting bodies provides insights into the changes during morphological development

Contact Info

Product

Resources

About