Identification and characterization of glucoamylase from the fungus, Thermomyces lanuginosus

Thor Seneca Thorsen; Anders Johnsen; K. Josefsen; Bo Jensen

doi:10.1016/j.bbapap.2006.01.009

Identification and characterization of glucoamylase from the fungus, Thermomyces lanuginosus

Thor Seneca Thorsen, Anders Johnsen, K. Josefsen, Bo Jensen

36 Citations (Scopus)

Abstract

The glucoamylase from the thermophilic fungus Thermomyces lanuginosus has a molecular weight of 66 kDa and was characterized with isoelectric point, pH and temperature optimum of 3.8-4.0, 5.0 and 70 °C, respectively. In addition, the activation energy is 60.4 kJ/mol, K_m is 3.5 mM and k_cat is 25.3 s^-1. The glucoamylase was partially sequenced on the protein level, and the complete glucoamylase gene including its promoter (but excluding its terminator region) was cloned and sequenced. The glucoamylase protein comprises 617 amino acid residues and shows 60% identity with the glucoamylase from the thermophilic fungus Talaromyces emersonii. cDNA encoding Thermomyces lanuginosus glucoamylase was expression cloned into Pichia pastoris, producing approximately 7.4 U/ml. It was concluded that alternative mRNA splicing as it might occur in Aspergillus niger glucoamylase is not responsible for the occurrence of different glucoamylase isoforms in Thermomyces lanuginosus.

Original language	English
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1764
Issue number	4
Pages (from-to)	671-676
ISSN	1570-9639
DOIs	https://doi.org/10.1016/j.bbapap.2006.01.009
Publication status	Published - 2006

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title = "Identification and characterization of glucoamylase from the fungus, Thermomyces lanuginosus",

abstract = "The glucoamylase from the thermophilic fungus Thermomyces lanuginosus has a molecular weight of 66 kDa and was characterized with isoelectric point, pH and temperature optimum of 3.8-4.0, 5.0 and 70 °C, respectively. In addition, the activation energy is 60.4 kJ/mol, Km is 3.5 mM and kcat is 25.3 s-1. The glucoamylase was partially sequenced on the protein level, and the complete glucoamylase gene including its promoter (but excluding its terminator region) was cloned and sequenced. The glucoamylase protein comprises 617 amino acid residues and shows 60% identity with the glucoamylase from the thermophilic fungus Talaromyces emersonii. cDNA encoding Thermomyces lanuginosus glucoamylase was expression cloned into Pichia pastoris, producing approximately 7.4 U/ml. It was concluded that alternative mRNA splicing as it might occur in Aspergillus niger glucoamylase is not responsible for the occurrence of different glucoamylase isoforms in Thermomyces lanuginosus.",

author = "Thorsen, {Thor Seneca} and Anders Johnsen and K. Josefsen and Bo Jensen",

note = "Keywords: Glucoamylase; Thermomyces lanuginosus; Cloning; Enzyme; Thermostability",

year = "2006",

doi = "10.1016/j.bbapap.2006.01.009",

language = "English",

volume = "1764",

pages = "671--676",

journal = "B B A - Proteins and Proteomics",

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TY - JOUR

T1 - Identification and characterization of glucoamylase from the fungus, Thermomyces lanuginosus

AU - Thorsen, Thor Seneca

AU - Johnsen, Anders

AU - Josefsen, K.

AU - Jensen, Bo

N1 - Keywords: Glucoamylase; Thermomyces lanuginosus; Cloning; Enzyme; Thermostability

PY - 2006

Y1 - 2006

N2 - The glucoamylase from the thermophilic fungus Thermomyces lanuginosus has a molecular weight of 66 kDa and was characterized with isoelectric point, pH and temperature optimum of 3.8-4.0, 5.0 and 70 °C, respectively. In addition, the activation energy is 60.4 kJ/mol, Km is 3.5 mM and kcat is 25.3 s-1. The glucoamylase was partially sequenced on the protein level, and the complete glucoamylase gene including its promoter (but excluding its terminator region) was cloned and sequenced. The glucoamylase protein comprises 617 amino acid residues and shows 60% identity with the glucoamylase from the thermophilic fungus Talaromyces emersonii. cDNA encoding Thermomyces lanuginosus glucoamylase was expression cloned into Pichia pastoris, producing approximately 7.4 U/ml. It was concluded that alternative mRNA splicing as it might occur in Aspergillus niger glucoamylase is not responsible for the occurrence of different glucoamylase isoforms in Thermomyces lanuginosus.

AB - The glucoamylase from the thermophilic fungus Thermomyces lanuginosus has a molecular weight of 66 kDa and was characterized with isoelectric point, pH and temperature optimum of 3.8-4.0, 5.0 and 70 °C, respectively. In addition, the activation energy is 60.4 kJ/mol, Km is 3.5 mM and kcat is 25.3 s-1. The glucoamylase was partially sequenced on the protein level, and the complete glucoamylase gene including its promoter (but excluding its terminator region) was cloned and sequenced. The glucoamylase protein comprises 617 amino acid residues and shows 60% identity with the glucoamylase from the thermophilic fungus Talaromyces emersonii. cDNA encoding Thermomyces lanuginosus glucoamylase was expression cloned into Pichia pastoris, producing approximately 7.4 U/ml. It was concluded that alternative mRNA splicing as it might occur in Aspergillus niger glucoamylase is not responsible for the occurrence of different glucoamylase isoforms in Thermomyces lanuginosus.

U2 - 10.1016/j.bbapap.2006.01.009

DO - 10.1016/j.bbapap.2006.01.009

M3 - Journal article

SN - 1570-9639

VL - 1764

SP - 671

EP - 676

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

IS - 4

ER -

Identification and characterization of glucoamylase from the fungus, Thermomyces lanuginosus

Abstract

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