Molecular Cloning of the Glucoamylase Gene of<i>Aspergillus shirousami</i>and Its Expression in<i>Aspergillus oryzae</i>

Shibuya, Ichiro; Gomi, Katsuya; Iimura, Yuzuru; Takahashi, Koichi; Tamura, Gakuzo; Hara, Shodo

doi:10.1080/00021369.1990.10870276

Cited by 3 publications

(2 citation statements)

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“…Transformation and cultivation for compound production: Inclusion of the ptrA gene allowed selection for A. oryzae transformants. A. oryzae transformation was carried out as described elsewhere,20 with modifications. Specifically, the recipient A. oryzae strain was initially cultivated in CD medium.…”

Section: Methodsmentioning

confidence: 99%

Overexpressing Transcriptional Regulator in Aspergillus oryzae Activates a Silent Biosynthetic Pathway to Produce a Novel Polyketide

et al. 2012

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Fungal genomes carry many gene clusters seemingly capable of natural product biosynthesis, yet most clusters remain silent. This places a major constraint on the conventional approach of cloning these genes in more amenable heterologous host for the natural product biosynthesis. One way to overcome this difficulty is to activate the silent gene clusters within the context of the target fungus. Here, we successfully activated a silent polyketide biosynthetic gene cluster in Aspergillus oryzae by overexpressing a transcriptional regulator found within the cluster from a plasmid. This strategy allowed us to isolate a new polyketide product and to efficiently decipher its biosynthetic pathway. Through this exercise, we also discovered unexpected activities of the biosynthetic enzymes found in the cluster. These results indicate that our approach would be valuable for isolating novel natural products and engineering analogues of comparable, if not more potent, bioactivity.

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Section: Methodsmentioning

confidence: 99%

Overexpressing Transcriptional Regulator in Aspergillus oryzae Activates a Silent Biosynthetic Pathway to Produce a Novel Polyketide

et al. 2012

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“…S3, ESI †). 18,19 Interestingly, while penilumamide A is a linear tripeptide, closer inspection of the three NRPSs, PlmA, PlmJ and PlmK, revealed a total of four modules, indicative of a tetrapeptide product. Thus, the activities of the monomodular PlmA and PlmK and dimodular PlmJ were reconstituted in vitro to verify if all three NPRSs were required for assembly of 1. plmA, plmJ and plmK were solubly expressed as recombinant C-terminal hexahistidyl-tagged proteins from Saccharomyces cerevisiae BJ5464-NpgA 20 (Fig.…”

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confidence: 99%

Biosynthesis of the fungal nonribosomal peptide penilumamide A and biochemical characterization of a pterin-specific adenylation domain

Heard,

Diehl,

Winter

2023

RSC Chem. Biol.

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Microbial glucoamylases: characteristics and applications

Kumar

Satyanarayana

2009

Critical Reviews in Biotechnology

161

111

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Glucoamylase is one of the oldest and widely used biocatalysts in food industry. The major application of glucoamylase is the saccharification of partially processed starch/dextrin to glucose, which is an essential substrate for numerous fermentation processes and a range of food and beverage industries. Glucoamylase for commercial purposes has traditionally been produced employing filamentous fungi, although a diverse group of microorganisms is reported to produce glucoamylase, since they secrete large quantities of the enzyme extracellularly. The commercially used fungal glucoamylases have certain limitations such as moderate thermostability, acidic pH requirement, and slow catalytic activity that increase the process cost. Consequently, the search for newer glucoamylases and protein engineering to improve pH and temperature optima leading to amelioration in catalytic efficiency of existing enzymes have been the major areas of research over the years. The present review focuses attention on the recent advances in molecular biology and protein engineering of glucoamylase to improve its production and functional properties including the so far success achieved in isolating mutants with enhanced thermostability and selectivity, higher pH optimum and improved catalytic activity. A comprehensive account is included on the diversity, regulation of production, classification, purification and properties, and potential applications of microbial glucoamylases to provide an overview on all the important aspects of the enzyme.

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Molecular Cloning of the Glucoamylase Gene ofAspergillus shirousamiand Its Expression inAspergillus oryzae

Cited by 3 publications

References 8 publications

Overexpressing Transcriptional Regulator in Aspergillus oryzae Activates a Silent Biosynthetic Pathway to Produce a Novel Polyketide

Overexpressing Transcriptional Regulator in Aspergillus oryzae Activates a Silent Biosynthetic Pathway to Produce a Novel Polyketide

Biosynthesis of the fungal nonribosomal peptide penilumamide A and biochemical characterization of a pterin-specific adenylation domain

Microbial glucoamylases: characteristics and applications

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