Purification and Properties of Two Forms of Glucoamylase from<i>Penicillium oxalicum</i>

Yamasaki, Yudai; Suzuki, Yukio; Ozawa, Junjiro

doi:10.1080/00021369.1977.10862579

Cited by 4 publications

(3 citation statements)

References 4 publications

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“…This value is higher than that reported for glucoamylase from other sources (Venkataramu et al, 1975;Yamasaki et al, 1977a;Taylor et al, 1978), an observation to be expected from the thermophilic nature of the organism. The activities of some enzymes from thermophilic organisms increased abruptly at about 500C, as shown by the breaks in the Arrhenius plots (Hachimori et al, 1970;Sugimoto & Nosoh, 1971;Middaugh et al, 1976).…”

Section: Thermal Stability Ofglucoamylasecontrasting

confidence: 53%

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Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus

Rao¹,

Sastri²,

Rao³

1981

Biochemical Journal

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Glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) was purified from the culture filtrates of the thermophilic fungus Thermomyces lanuginosus and was established to be homogeneous by a number of criteria. The enzyme was a glycoprotein with an average molecular weight of about 57 000 and a carbohydrate content of 10-12%. The enzyme hydrolysed successive glucose residues from the non-reducing ends of the starch molecule. It did not exhibit any glucosyltransferase activity. The enzyme appeared to hydrolyse maltotriose by the multi-chain mechanism. The enzyme was unable to hydrolyse 1,6-alpha-D-glucosidic linkages of isomaltose and dextran. It was optimally active at 70 degrees C. The enzyme exhibited increase in the Vmax. and decreased in Km values with increasing chain length of the substrate molecule. The enzyme was inhibited by the substrate analogue D-glucono-delta-lactone in a non-competitive manner. The enzyme inhibited remarkable resistance towards chemical and thermal denaturation.

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Section: Thermal Stability Ofglucoamylasecontrasting

confidence: 53%

“…It was also shown to exist in two or more isoenzymic forms in Aspergillus niger (Venkataramu et al, 1975), Penicillium oxalicum (Yamasaki et al, 1977a), Mucor rouxianus (Tsuboi et al, 1974) and several other fungi (Takahashi et al, 1978;lizuka & Mineki, 1977;Razzaque & Ueda, 1978).…”

mentioning

confidence: 99%

Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus

Rao¹,

Sastri²,

Rao³

1981

Biochemical Journal

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“…l ) Glucoamylase activity was determined under the same conditions as employed in the assay for the a-glucosidase activity, except that soluble starch was used in place of maltose. 7 ) Determination of protein.…”

Section: Methodsmentioning

confidence: 99%

Purification and Properties of α-Glucosidase and Glucoamylase fromLentinus edodes (Berk.) Sing.

Yamasaki

Suzuki

1978

Agricultural and Biological Chemistry

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Microbial glucoamylases: characteristics and applications

Kumar

Satyanarayana

2009

Critical Reviews in Biotechnology

164

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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Purification and Properties of Two Forms of Glucoamylase fromPenicillium oxalicum

Cited by 4 publications

References 4 publications

Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus

Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus

Purification and Properties of α-Glucosidase and Glucoamylase fromLentinus edodes (Berk.) Sing.

Microbial glucoamylases: characteristics and applications

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