Production, purification, and characterization of Thermoanaerobacterium thermosaccharolyticum glucoamylase

Ping Hua Feng; Sonja Berensmeier; Klaus Buchholz; Peter J. Reilly

doi:10.1002/1521-379X(200208)54:8<328::AID-STAR328>3.0.CO;2-7

Production, purification, and characterization of Thermoanaerobacterium thermosaccharolyticum glucoamylase

Ping Hua Feng, Sonja Berensmeier, Klaus Buchholz, Peter J. Reilly

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Glucoamylase from Thermoanaerobacterium thermosaccharolyticum ATCC 7956 (DSM 571) was produced in extracellular form. It was purified to homogeneity by two separate methods, one with two chromatographic steps and the other with three. This glucoamylase is closely related to glucoamylases from Clostridium sp. G0005 and T. thermosaccharolyticum DSM 572. Activities and K_M values with maltose substrate are less than one-tenth and about fourfold, respectively, those of Aspergillus niger glucoamylase. T. thermosaccharolyticum glucoamylase is about twenty times as thermostable as A. niger glucoamylase and its optimal pH is somewhat higher at 4.9; however, it is produced in much lower activities. Sorbitol strongly stabilizes A. niger glucoamylase.

Original language	English
Pages (from-to)	328-337
Number of pages	10
Journal	Starch/Staerke
Volume	54
Issue number	8
DOIs	https://doi.org/10.1002/1521-379X(200208)54:8<328::AID-STAR328>3.0.CO;2-7
State	Published - Aug 2002
Externally published	Yes

Keywords

Aspergillus niger
Characterization
Glucoamylase
Kinetics
Production
Purification
Sorbitol
Th ermoanaerobacterium thermosaccharolyticum
Thermostability

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10.1002/1521-379X(200208)54:8<328::AID-STAR328>3.0.CO;2-7

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title = "Production, purification, and characterization of Thermoanaerobacterium thermosaccharolyticum glucoamylase",

abstract = "Glucoamylase from Thermoanaerobacterium thermosaccharolyticum ATCC 7956 (DSM 571) was produced in extracellular form. It was purified to homogeneity by two separate methods, one with two chromatographic steps and the other with three. This glucoamylase is closely related to glucoamylases from Clostridium sp. G0005 and T. thermosaccharolyticum DSM 572. Activities and KM values with maltose substrate are less than one-tenth and about fourfold, respectively, those of Aspergillus niger glucoamylase. T. thermosaccharolyticum glucoamylase is about twenty times as thermostable as A. niger glucoamylase and its optimal pH is somewhat higher at 4.9; however, it is produced in much lower activities. Sorbitol strongly stabilizes A. niger glucoamylase.",

keywords = "Aspergillus niger, Characterization, Glucoamylase, Kinetics, Production, Purification, Sorbitol, Th ermoanaerobacterium thermosaccharolyticum, Thermostability",

author = "Feng, {Ping Hua} and Sonja Berensmeier and Klaus Buchholz and Reilly, {Peter J.}",

year = "2002",

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TY - JOUR

T1 - Production, purification, and characterization of Thermoanaerobacterium thermosaccharolyticum glucoamylase

AU - Feng, Ping Hua

AU - Berensmeier, Sonja

AU - Buchholz, Klaus

AU - Reilly, Peter J.

PY - 2002/8

Y1 - 2002/8

N2 - Glucoamylase from Thermoanaerobacterium thermosaccharolyticum ATCC 7956 (DSM 571) was produced in extracellular form. It was purified to homogeneity by two separate methods, one with two chromatographic steps and the other with three. This glucoamylase is closely related to glucoamylases from Clostridium sp. G0005 and T. thermosaccharolyticum DSM 572. Activities and KM values with maltose substrate are less than one-tenth and about fourfold, respectively, those of Aspergillus niger glucoamylase. T. thermosaccharolyticum glucoamylase is about twenty times as thermostable as A. niger glucoamylase and its optimal pH is somewhat higher at 4.9; however, it is produced in much lower activities. Sorbitol strongly stabilizes A. niger glucoamylase.

AB - Glucoamylase from Thermoanaerobacterium thermosaccharolyticum ATCC 7956 (DSM 571) was produced in extracellular form. It was purified to homogeneity by two separate methods, one with two chromatographic steps and the other with three. This glucoamylase is closely related to glucoamylases from Clostridium sp. G0005 and T. thermosaccharolyticum DSM 572. Activities and KM values with maltose substrate are less than one-tenth and about fourfold, respectively, those of Aspergillus niger glucoamylase. T. thermosaccharolyticum glucoamylase is about twenty times as thermostable as A. niger glucoamylase and its optimal pH is somewhat higher at 4.9; however, it is produced in much lower activities. Sorbitol strongly stabilizes A. niger glucoamylase.

KW - Aspergillus niger

KW - Characterization

KW - Glucoamylase

KW - Kinetics

KW - Production

KW - Purification

KW - Sorbitol

KW - Th ermoanaerobacterium thermosaccharolyticum

KW - Thermostability

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U2 - 10.1002/1521-379X(200208)54:8<328::AID-STAR328>3.0.CO;2-7

DO - 10.1002/1521-379X(200208)54:8<328::AID-STAR328>3.0.CO;2-7

M3 - Article

AN - SCOPUS:0036686358

SN - 0038-9056

VL - 54

SP - 328

EP - 337

JO - Starch/Staerke

JF - Starch/Staerke

IS - 8

ER -

Production, purification, and characterization of Thermoanaerobacterium thermosaccharolyticum glucoamylase

Abstract

Keywords

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