Endo-β-glucosidase from Aspergillus niger grown on a monoterpene glycoside-containing medium

Oded Shoseyov; Ben Ami Bravdo; Raphael Ikan; Ilan Chet

doi:10.1016/0031-9422(88)80080-3

Endo-β-glucosidase from Aspergillus niger grown on a monoterpene glycoside-containing medium

Oded Shoseyov, Ben Ami Bravdo, Raphael Ikan, Ilan Chet

Institute of Plant Sciences and Genetics in Agriculture

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

39 Scopus citations

Abstract

An endo-β-glucosidase was isolated from Aspergillus niger grown on a medium containing rutin as the sole carbon source, and was partially purified by affinity chromatography. The enzyme was found to be extracellular. Its optimum pH was 3.4, and its optimum temperature 65°. K_M values were 1 mM (PNPG) and 1.25 mM (geranyl-β-rutinoside), V_max values were 0.22 μmol/min/mg protein (PNPG) and 0.08 μmol/min/mg protein (geranyl-β-rutinoside), and K_I was 40 mM (glucose). The enzyme's activity was not inhibited by fructose, sucrose or SO₂, and was enhanced by ethanol. No loss of activity was found after seven days at 50°. M_r determined by gel filtration was 120 000. Using polyacrylamide isoelectric focusing gel, a pI of 3.9 was obtained.

Original language	English
Pages (from-to)	1973-1976
Number of pages	4
Journal	Phytochemistry
Volume	27
Issue number	7
DOIs	https://doi.org/10.1016/0031-9422(88)80080-3
State	Published - 1988

Keywords

Aspergillus niger, Vitis vinifera
monoterpene glycosides
wine
β-glucosidase.

Access to Document

10.1016/0031-9422(88)80080-3

Cite this

@article{669e0d985a514b18ba3db8c0d6a2ef04,

title = "Endo-β-glucosidase from Aspergillus niger grown on a monoterpene glycoside-containing medium",

abstract = "An endo-β-glucosidase was isolated from Aspergillus niger grown on a medium containing rutin as the sole carbon source, and was partially purified by affinity chromatography. The enzyme was found to be extracellular. Its optimum pH was 3.4, and its optimum temperature 65°. KM values were 1 mM (PNPG) and 1.25 mM (geranyl-β-rutinoside), Vmax values were 0.22 μmol/min/mg protein (PNPG) and 0.08 μmol/min/mg protein (geranyl-β-rutinoside), and KI was 40 mM (glucose). The enzyme's activity was not inhibited by fructose, sucrose or SO2, and was enhanced by ethanol. No loss of activity was found after seven days at 50°. Mr determined by gel filtration was 120 000. Using polyacrylamide isoelectric focusing gel, a pI of 3.9 was obtained.",

keywords = "Aspergillus niger, Vitis vinifera, monoterpene glycosides, wine, β-glucosidase.",

author = "Oded Shoseyov and Bravdo, {Ben Ami} and Raphael Ikan and Ilan Chet",

year = "1988",

doi = "10.1016/0031-9422(88)80080-3",

language = "אנגלית",

volume = "27",

pages = "1973--1976",

journal = "Phytochemistry",

issn = "0031-9422",

publisher = "Elsevier Ltd.",

number = "7",

}

TY - JOUR

T1 - Endo-β-glucosidase from Aspergillus niger grown on a monoterpene glycoside-containing medium

AU - Shoseyov, Oded

AU - Bravdo, Ben Ami

AU - Ikan, Raphael

AU - Chet, Ilan

PY - 1988

Y1 - 1988

N2 - An endo-β-glucosidase was isolated from Aspergillus niger grown on a medium containing rutin as the sole carbon source, and was partially purified by affinity chromatography. The enzyme was found to be extracellular. Its optimum pH was 3.4, and its optimum temperature 65°. KM values were 1 mM (PNPG) and 1.25 mM (geranyl-β-rutinoside), Vmax values were 0.22 μmol/min/mg protein (PNPG) and 0.08 μmol/min/mg protein (geranyl-β-rutinoside), and KI was 40 mM (glucose). The enzyme's activity was not inhibited by fructose, sucrose or SO2, and was enhanced by ethanol. No loss of activity was found after seven days at 50°. Mr determined by gel filtration was 120 000. Using polyacrylamide isoelectric focusing gel, a pI of 3.9 was obtained.

AB - An endo-β-glucosidase was isolated from Aspergillus niger grown on a medium containing rutin as the sole carbon source, and was partially purified by affinity chromatography. The enzyme was found to be extracellular. Its optimum pH was 3.4, and its optimum temperature 65°. KM values were 1 mM (PNPG) and 1.25 mM (geranyl-β-rutinoside), Vmax values were 0.22 μmol/min/mg protein (PNPG) and 0.08 μmol/min/mg protein (geranyl-β-rutinoside), and KI was 40 mM (glucose). The enzyme's activity was not inhibited by fructose, sucrose or SO2, and was enhanced by ethanol. No loss of activity was found after seven days at 50°. Mr determined by gel filtration was 120 000. Using polyacrylamide isoelectric focusing gel, a pI of 3.9 was obtained.

KW - Aspergillus niger, Vitis vinifera

KW - monoterpene glycosides

KW - wine

KW - β-glucosidase.

UR - http://www.scopus.com/inward/record.url?scp=0000684688&partnerID=8YFLogxK

U2 - 10.1016/0031-9422(88)80080-3

DO - 10.1016/0031-9422(88)80080-3

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0000684688

SN - 0031-9422

VL - 27

SP - 1973

EP - 1976

JO - Phytochemistry

JF - Phytochemistry

IS - 7

ER -

Endo-β-glucosidase from Aspergillus niger grown on a monoterpene glycoside-containing medium

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this