Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)

Josep A. Pérez-Pons; Xavier Rebordosa; Enrique Querol

doi:10.1016/0167-4838(95)00074-5

Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)

Josep A. Pérez-Pons, Xavier Rebordosa, Enrique Querol

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

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Abstract

An inducible intracellular β-glucosidase (EC 3.2.1.21) from Streptomyces sp. QM-B814 (ATCC 11238) has been purified and characterized. The purified polypeptide is monomeric with a relative molecular mass of 62 kDa by SDS-PAGE and 42 kDa by size-exclusion chromatography; its isoelectric point is 4.2. The difference in the molecular mass values can be attributed to the glycosylated nature of the protein. The purified enzyme has a pH optimum of 6.0-6.5. The temperature optimum for activity is 50°C; at this temperature the enzyme is stable for 1 h. The enzyme hydrolyzes mainly aryl-β-glucosides but also presents significant activity against β-linked disaccharides and maltose. The enzyme displays an unusual kinetic behavior and biphasic Lineweaver-Burk and Eadie-Hofstee plots for p-nitrophenyl-β-d-glucoside and cellobiose were obtained. The enzyme presents β-glycosyltransferase activity and an exoglycosidase-type action on cellodextrins. It is inhibited by δ-gluconolactone (Ki 0.44 mM) but, remarkably, glucose in the range 25-200 mM enhances the rate of p-nitrophenyl-β-d-glucoside hydrolysis. © 1995.

Original language	English
Pages (from-to)	145-153
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	1251
Issue number	2
DOIs	https://doi.org/10.1016/0167-4838(95)00074-5
Publication status	Published - 6 Sep 1995

Keywords

(Streptomycete)
Characterization
Glucose-enhanced glucosidase
Purification
β-Glucosidase

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title = "Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)",

abstract = "An inducible intracellular β-glucosidase (EC 3.2.1.21) from Streptomyces sp. QM-B814 (ATCC 11238) has been purified and characterized. The purified polypeptide is monomeric with a relative molecular mass of 62 kDa by SDS-PAGE and 42 kDa by size-exclusion chromatography; its isoelectric point is 4.2. The difference in the molecular mass values can be attributed to the glycosylated nature of the protein. The purified enzyme has a pH optimum of 6.0-6.5. The temperature optimum for activity is 50°C; at this temperature the enzyme is stable for 1 h. The enzyme hydrolyzes mainly aryl-β-glucosides but also presents significant activity against β-linked disaccharides and maltose. The enzyme displays an unusual kinetic behavior and biphasic Lineweaver-Burk and Eadie-Hofstee plots for p-nitrophenyl-β-d-glucoside and cellobiose were obtained. The enzyme presents β-glycosyltransferase activity and an exoglycosidase-type action on cellodextrins. It is inhibited by δ-gluconolactone (Ki 0.44 mM) but, remarkably, glucose in the range 25-200 mM enhances the rate of p-nitrophenyl-β-d-glucoside hydrolysis. {\textcopyright} 1995.",

keywords = "(Streptomycete), Characterization, Glucose-enhanced glucosidase, Purification, β-Glucosidase",

author = "P{\'e}rez-Pons, {Josep A.} and Xavier Rebordosa and Enrique Querol",

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T1 - Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)

AU - Pérez-Pons, Josep A.

AU - Rebordosa, Xavier

AU - Querol, Enrique

PY - 1995/9/6

Y1 - 1995/9/6

N2 - An inducible intracellular β-glucosidase (EC 3.2.1.21) from Streptomyces sp. QM-B814 (ATCC 11238) has been purified and characterized. The purified polypeptide is monomeric with a relative molecular mass of 62 kDa by SDS-PAGE and 42 kDa by size-exclusion chromatography; its isoelectric point is 4.2. The difference in the molecular mass values can be attributed to the glycosylated nature of the protein. The purified enzyme has a pH optimum of 6.0-6.5. The temperature optimum for activity is 50°C; at this temperature the enzyme is stable for 1 h. The enzyme hydrolyzes mainly aryl-β-glucosides but also presents significant activity against β-linked disaccharides and maltose. The enzyme displays an unusual kinetic behavior and biphasic Lineweaver-Burk and Eadie-Hofstee plots for p-nitrophenyl-β-d-glucoside and cellobiose were obtained. The enzyme presents β-glycosyltransferase activity and an exoglycosidase-type action on cellodextrins. It is inhibited by δ-gluconolactone (Ki 0.44 mM) but, remarkably, glucose in the range 25-200 mM enhances the rate of p-nitrophenyl-β-d-glucoside hydrolysis. © 1995.

AB - An inducible intracellular β-glucosidase (EC 3.2.1.21) from Streptomyces sp. QM-B814 (ATCC 11238) has been purified and characterized. The purified polypeptide is monomeric with a relative molecular mass of 62 kDa by SDS-PAGE and 42 kDa by size-exclusion chromatography; its isoelectric point is 4.2. The difference in the molecular mass values can be attributed to the glycosylated nature of the protein. The purified enzyme has a pH optimum of 6.0-6.5. The temperature optimum for activity is 50°C; at this temperature the enzyme is stable for 1 h. The enzyme hydrolyzes mainly aryl-β-glucosides but also presents significant activity against β-linked disaccharides and maltose. The enzyme displays an unusual kinetic behavior and biphasic Lineweaver-Burk and Eadie-Hofstee plots for p-nitrophenyl-β-d-glucoside and cellobiose were obtained. The enzyme presents β-glycosyltransferase activity and an exoglycosidase-type action on cellodextrins. It is inhibited by δ-gluconolactone (Ki 0.44 mM) but, remarkably, glucose in the range 25-200 mM enhances the rate of p-nitrophenyl-β-d-glucoside hydrolysis. © 1995.

KW - (Streptomycete)

KW - Characterization

KW - Glucose-enhanced glucosidase

KW - Purification

KW - β-Glucosidase

U2 - 10.1016/0167-4838(95)00074-5

DO - 10.1016/0167-4838(95)00074-5

M3 - Article

VL - 1251

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