Purification of soluble invertase from potato

L. R. Burch; H. V. Davies; E. M. Cuthbert; E. C. Machray; P. Hedley; R. Waugh

doi:10.1016/0031-9422(92)80331-8

Purification of soluble invertase from potato

L. R. Burch (Lead / Corresponding author), H. V. Davies, E. M. Cuthbert, E. C. Machray, P. Hedley, R. Waugh

Plant Sciences

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

22 Citations (Scopus)

Abstract

Proteins with acid invertase activity have been identified from potato (Solanum tuberosum L.) leaves and tubers, and purified to near homogeneity. Under denaturing conditions (SDS-PAGE) the purified invertase is associated in each case with a 58 000 M_r polypeptide. A pI of pH 5.2 was determined for the tuber enzyme and both invertases had a pH optimum of 5. The K_m (sucrose) was 7.9 mM for the tuber enzyme and 2.4 mM for the leaf enzyme. In addition, leaf invertase also hydrolysed lactose (K_m 6.4 mM) at approximately 10% of the rate of sucrose. Tuber invertase also hydrolysed lactose (K_m 9.2 mM), raffinose (K_m 7.1 mM) and trehalose (K_m 0.66 mM), again at a rate approximately 10% that of sucrose. Product inhibition by fructose was linear mixed for the leaf enzyme and competitive for the tuber enzyme. Glucose inhibition was uncompetitive for the leaf enzyme and non-competitive for tuber invertase.

Original language	English
Pages (from-to)	1901-1904
Number of pages	4
Journal	Phytochemistry
Volume	31
Issue number	6
DOIs	https://doi.org/10.1016/0031-9422(92)80331-8
Publication status	Published - 1 Jun 1992

Keywords

invertase
potato
purification.
Solanaceae
Solanum tuberosum

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Plant Science
Horticulture

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10.1016/0031-9422(92)80331-8

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title = "Purification of soluble invertase from potato",

abstract = "Proteins with acid invertase activity have been identified from potato (Solanum tuberosum L.) leaves and tubers, and purified to near homogeneity. Under denaturing conditions (SDS-PAGE) the purified invertase is associated in each case with a 58 000 Mr polypeptide. A pI of pH 5.2 was determined for the tuber enzyme and both invertases had a pH optimum of 5. The Km (sucrose) was 7.9 mM for the tuber enzyme and 2.4 mM for the leaf enzyme. In addition, leaf invertase also hydrolysed lactose (Km 6.4 mM) at approximately 10% of the rate of sucrose. Tuber invertase also hydrolysed lactose (Km 9.2 mM), raffinose (Km 7.1 mM) and trehalose (Km 0.66 mM), again at a rate approximately 10% that of sucrose. Product inhibition by fructose was linear mixed for the leaf enzyme and competitive for the tuber enzyme. Glucose inhibition was uncompetitive for the leaf enzyme and non-competitive for tuber invertase.",

keywords = "invertase, potato, purification., Solanaceae, Solanum tuberosum",

author = "Burch, {L. R.} and Davies, {H. V.} and Cuthbert, {E. M.} and Machray, {E. C.} and P. Hedley and R. Waugh",

year = "1992",

month = jun,

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doi = "10.1016/0031-9422(92)80331-8",

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T1 - Purification of soluble invertase from potato

AU - Burch, L. R.

AU - Davies, H. V.

AU - Cuthbert, E. M.

AU - Machray, E. C.

AU - Hedley, P.

AU - Waugh, R.

PY - 1992/6/1

Y1 - 1992/6/1

N2 - Proteins with acid invertase activity have been identified from potato (Solanum tuberosum L.) leaves and tubers, and purified to near homogeneity. Under denaturing conditions (SDS-PAGE) the purified invertase is associated in each case with a 58 000 Mr polypeptide. A pI of pH 5.2 was determined for the tuber enzyme and both invertases had a pH optimum of 5. The Km (sucrose) was 7.9 mM for the tuber enzyme and 2.4 mM for the leaf enzyme. In addition, leaf invertase also hydrolysed lactose (Km 6.4 mM) at approximately 10% of the rate of sucrose. Tuber invertase also hydrolysed lactose (Km 9.2 mM), raffinose (Km 7.1 mM) and trehalose (Km 0.66 mM), again at a rate approximately 10% that of sucrose. Product inhibition by fructose was linear mixed for the leaf enzyme and competitive for the tuber enzyme. Glucose inhibition was uncompetitive for the leaf enzyme and non-competitive for tuber invertase.

AB - Proteins with acid invertase activity have been identified from potato (Solanum tuberosum L.) leaves and tubers, and purified to near homogeneity. Under denaturing conditions (SDS-PAGE) the purified invertase is associated in each case with a 58 000 Mr polypeptide. A pI of pH 5.2 was determined for the tuber enzyme and both invertases had a pH optimum of 5. The Km (sucrose) was 7.9 mM for the tuber enzyme and 2.4 mM for the leaf enzyme. In addition, leaf invertase also hydrolysed lactose (Km 6.4 mM) at approximately 10% of the rate of sucrose. Tuber invertase also hydrolysed lactose (Km 9.2 mM), raffinose (Km 7.1 mM) and trehalose (Km 0.66 mM), again at a rate approximately 10% that of sucrose. Product inhibition by fructose was linear mixed for the leaf enzyme and competitive for the tuber enzyme. Glucose inhibition was uncompetitive for the leaf enzyme and non-competitive for tuber invertase.

KW - invertase

KW - potato

KW - purification.

KW - Solanaceae

KW - Solanum tuberosum

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VL - 31

SP - 1901

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JO - Phytochemistry

JF - Phytochemistry

IS - 6

ER -

Purification of soluble invertase from potato

Abstract

Keywords

ASJC Scopus subject areas

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