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An investigation of the kinetics and...

Maghasi, Anna Tamnai Chemsito.

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An investigation of the kinetics and inhibition of pectinesterase.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	An investigation of the kinetics and inhibition of pectinesterase./
作者:	Maghasi, Anna Tamnai Chemsito.
面頁冊數:	73 p.
附註:	Source: Masters Abstracts International, Volume: 39-04, page: 1160.
Contained By:	Masters Abstracts International39-04.
標題:	Chemistry, Analytical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1402891
ISBN:	0493087699

An investigation of the kinetics and inhibition of pectinesterase.
Maghasi, Anna Tamnai Chemsito.

An investigation of the kinetics and inhibition of pectinesterase. - 73 p.

Source: Masters Abstracts International, Volume: 39-04, page: 1160.

Thesis (M.S.)--Michigan State University, 2000.

Methanol in fruit brandy is regulated by the FDA because of its toxic properties. To reduce the amount of methanol in fruit brandy, it is necessary to understand the source and mode of its generation. Pectinesterase enzyme is responsible for the deesterification of fruit pectin and generates methanol as one of the major products. The kinetics of pectinesterase and its inactivation by heat were studied. At 70°C, Pectinesterase was found to be inactivated significantly with an inactivation rate constant of 2.8 x 10 -3s-1.

ISBN: 0493087699Subjects--Topical Terms:

586156
Chemistry, Analytical.

An investigation of the kinetics and inhibition of pectinesterase.
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245 1 3 $a An investigation of the kinetics and inhibition of pectinesterase.
300 $a 73 p.
500 $a Source: Masters Abstracts International, Volume: 39-04, page: 1160.
502 $a Thesis (M.S.)--Michigan State University, 2000.
520 $a Methanol in fruit brandy is regulated by the FDA because of its toxic properties. To reduce the amount of methanol in fruit brandy, it is necessary to understand the source and mode of its generation. Pectinesterase enzyme is responsible for the deesterification of fruit pectin and generates methanol as one of the major products. The kinetics of pectinesterase and its inactivation by heat were studied. At 70°C, Pectinesterase was found to be inactivated significantly with an inactivation rate constant of 2.8 x 10 -3s-1.
520 $a Various inhibitors were tested for their effect on the activity of pectinesterase. Tannic acid, polyacrylic acid, polymaleimide, citric acid and ethylenediamminetetraacetic acid (EDTA) were tested as potential inhibitors. Polyacrylic acid was found to reduce the activity of pectinesterase by nearly 45%. EDTA also significantly reduced the amount of methanol generated by pectinesterase. It is postulated that they act by providing excess carboxylate functionality thereby shifting the equilibrium of the deesterification reaction.
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650 4 $a Agriculture, Food Science and Technology. $3 1017813
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