Purification and Characterization of Heterogeneous Glucoamylases from<i>Monascus purpureus</i>

Tachibana, Sanro; Yasuda, Masaaki

doi:10.1271/bbb.70285

Cited by 23 publications

(10 citation statements)

References 26 publications

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“…In tofuyo production, glucoamylases play an important role in providing taste to the product. Two forms of an extracellular glucoamylase, MpuGA-I and MpuGA-II, were purified to homogeneity from M. purpureus in our laboratory (Tachibana & Yasuda, 2007). The properties of the enzyme were summarized as follows.…”

Section: Characterization Of Glucoamylases From Genus Monascusmentioning

confidence: 99%

Fermented Tofu, Tofuyo

Yasuda¹

2011

Soybean - Biochemistry, Chemistry and Physiology

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Section: Characterization Of Glucoamylases From Genus Monascusmentioning

confidence: 99%

Fermented Tofu, Tofuyo

Yasuda¹

2011

Soybean - Biochemistry, Chemistry and Physiology

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“…The possible reason is that the glycosylation status of the native protein is more Li et al 9127 beneficial to its thermostability. Optimal temperature of glucoamylase from Chaetomium thermophilum is 65°C (Chen et al, 2007), however, the glucoamylase MpuGA-I from Monascus purpureus RY3410 has an optimal temperature of 50°C (Tachibana and Yasuda, 2007). So, among other fungal glucoamylase, the thermostabilty of APGA1 is relatively intermediate.…”

Section: Recombinant Expression Purification and Characterisationmentioning

confidence: 99%

Cloning, recombinant expression and characterization of a new glucoamylase gene from Aureobasidium pullulans NRRL 12974 and its potential application in raw potato starch degradation

Li¹,

Sun²,

Huang³

et al. 2011

Afr. J. Biotechnol.

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A new amylase gene APGA1 was cloned from Aureobasidium pullulans NRRL 12974 and expressed in Pichia pastoris. This is the first report on cloning and expression of amylolytic gene from the industrially important microorganism A. pullulans. The purified recombinant protein with MW of 66 kDa and specific activity of 298.02 Umg-1 protein was verified as a glucoamylase by its hydrolytic mode. This recombinant glucoamylase with optimal pH of 4.5, and temperature of 60°C, showed good hydrolytic activity against raw potato starch. At 60°C, 83.1% of raw potato starch slurry (150 gl-1) was hydrolysed into glucose by 0.1 U mg-1 starch purified recombinant glucoamylase in less than 2.5 h. This is the highest raw starch hydrolysis efficiency report about recombinant fungal glucoamylase. This useful property indicated that this glucoamylase may find important applications in the starch saccharification industry and in bioethanol production.

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“…M . purpureus metabolic components include bioactive compounds [1–3] such as pigments [4], monacolin K [5–7], citrinin [8], aminobutyric acid [9], ergosterol, toxins and other metabolites [10,11], hydrolytic enzymes [12] that are involved in a wide range of activities [13,14] and are used as ingredients in food coloring [15,16], wine and pharmaceuticals.…”

Section: Introductionmentioning

confidence: 99%

De Novo RNA Sequencing and Transcriptome Analysis of Monascus purpureus and Analysis of Key Genes Involved in Monacolin K Biosynthesis

Zhang

Liang²,

Yang³

et al. 2017

PLoS ONE

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Monascus purpureus is an important medicinal and edible microbial resource. To facilitate biological, biochemical, and molecular research on medicinal components of M. purpureus, we investigated the M. purpureus transcriptome by RNA sequencing (RNA-seq). An RNA-seq library was created using RNA extracted from a mixed sample of M. purpureus expressing different levels of monacolin K output. In total 29,713 unigenes were assembled from more than 60 million high-quality short reads. A BLAST search revealed hits for 21,331 unigenes in at least one of the protein or nucleotide databases used in this study. The 22,365 unigenes were categorized into 48 functional groups based on Gene Ontology classification. Owing to the economic and medicinal importance of M. purpureus, most studies on this organism have focused on the pharmacological activity of chemical components and the molecular function of genes involved in their biogenesis. In this study, we performed quantitative real-time PCR to detect the expression of genes related to monacolin K (mokA-mokI) at different phases (2, 5, 8, and 12 days) of M. purpureus M1 and M1-36. Our study found that mokF modulates monacolin K biogenesis in M. purpureus. Nine genes were suggested to be associated with the monacolin K biosynthesis. Studies on these genes could provide useful information on secondary metabolic processes in M. purpureus. These results indicate a detailed resource through genetic engineering of monacolin K biosynthesis in M. purpureus and related species.

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Purification and Characterization of Heterogeneous Glucoamylases fromMonascus purpureus

Cited by 23 publications

References 26 publications

Fermented Tofu, Tofuyo

Fermented Tofu, Tofuyo

Cloning, recombinant expression and characterization of a new glucoamylase gene from Aureobasidium pullulans NRRL 12974 and its potential application in raw potato starch degradation

De Novo RNA Sequencing and Transcriptome Analysis of Monascus purpureus and Analysis of Key Genes Involved in Monacolin K Biosynthesis

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