Coin handling – Deliverer – Delivery of a distinct number of plural coins from a single...
Patent
1997-07-02
1999-01-12
Wax, Robert A.
Coin handling
Deliverer
Delivery of a distinct number of plural coins from a single...
43525411, 4352543, 4352523, 43525233, 4353201, 536 232, 536 2374, C12N 988
Patent
active
058587608
DESCRIPTION:
BRIEF SUMMARY
FIELD OF INVENTION
The present invention relates to an enzyme with pectin lyase activity, a method of producing the enzyme, and an enzyme preparation containing the enzyme.
BACKGROUND OF THE INVENTION
Pectin polymers are important constituents of plant primary cell walls. They are composed of chains of 1,4-linked .alpha.-D-galacturonic acid and methylated derivatives thereof. The use of pectin-degrading enzymes is important for the food industry, primarily in fruit and vegetable processing such as fruit juice production or wine making, where their ability to catalyse the degradation of the backbone of the pectin polymer is utilised.
An assortment of different pectin degrading enzymes is known to be present in various microorganisms such as Aspergillus niger. Of these, pectin methylesterase catalyses the removal of methanol from pectin, resulting in the formation of pectic acid (polygalacturonic acid). Pectate lyase cleaves glycosidic bonds in polygalacturonic acid by .beta.-elimination, pectin lyase cleaves the glycosidic bonds of highly methylated pectins by .beta.-elimination, and polygalacturonase hydrolyses the glycosidic linkages in the polygalacturonic acid chain.
More specifically, pectin lyase may be used, alone or in combination with one or more other pectin degrading enzymes, in the production of fruit juice, in particular citrus juice, for partial or complete degradation of the pulp present in the juice after pressing.
For many purposes, it would be desirable to provide each of the pectin degrading enzymes present in, for instance, commercial preparations containing a number of different pectin degrading enzymes (an example of such a preparation is Pectinex Ultra SP.RTM., prepared from Aspergillus aculeatus, available from Novo Nordisk A/S) in a form free from other components. In this way, it would be possible to produce enzyme preparations adapted to specific purposes, such preparations either containing a single pectin degrading enzyme or arbitrary combinations thereof. To serve this end, it is convenient to provide single-component pectin degrading enzymes by recombinant DNA techniques.
Plastow et al., Symbiosis 2, 1986, pp. 115-122, describe the cloning of four pectate lyase genes and one polygalacturonase gene from Erwinia in E. coli.
Cloning of a pectin lyase is described in EP 278 355 and EP 353 188.
M. Kusters-van Sommeren et al., Mol. Gen. Genet. 234, 1992, pp. 113-120, describe the nucleotide sequence of the Aspergillus niger pelB gene encoding pectin lyase B.
C. Gysler et al., Gene 89, 1990, pp. 101-108, describe the isolation and nucleotide sequence of the Aspergillus niger pelD gene encoding pectin lyase D.
A. Alana et al., FEBS Letters 280, 1991, pp. 335-340, describe the purification and some characteristics of a pectin lyase from Penicillium italicum.
SUMMARY OF THE INVENTION
It is an object of the present invention to prepare single-component pectin lyases.
Accordingly, the present invention relates to an enzyme exhibiting pectin lyase activity, which enzyme is immunologically reactive with an antibody raised against a purified pectin lyase derived from Aspergillus aculeatus, CBS 101.43.
In the present context, the term "derived from" is intended not only to indicate a pectin lyase produced by strain CBS 101.43, but also a pectin lyase encoded by a DNA sequence isolated from strain CBS 101.43 and produced in a host organism transformed with said DNA sequence.
In another aspect, the invention relates to an enzyme exhibiting pectin lyase activity, which enzyme is encoded by a DNA sequence comprising at least one of the following partial sequences
______________________________________ (a) CGATAAACTG CAATATGGCA (SEQ ID NO: 1)
(b) TTGACCACGA TGGCTCAGGT (SEQ ID NO: 2)
(c) CTTTGGCCGT TGGCCCAGCT (SEQ ID NO: 3)
(d) CGCCACAGCT GTGAGTGTTT (SEQ ID NO: 4)
(e) CCGGTGCGGC AGAGGGCTTC (SEQ ID NO: 5)
(f) GCAAAAGGTG TCACTGGTGG (SEQ ID NO: 6)
(g) TGGTAGTGCG ACTCCGGTTT (SEQ ID NO: 7)
(h) ATCTACCACG ACTGATGAGC (SEQ ID NO: 8)
(i) TGGTCTCCTA CCTCGGTGAC TCTT (SEQ ID NO: 9)
(j) GCATTG
REFERENCES:
patent: 5103883 (1992-04-01), Viikari et al.
patent: 5447862 (1995-09-01), Heim et al.
Plastow et al., Symbiosis, vol. 2, pp. 115-122, 1986.
Somersen et al., Mol. Gen. Genet., vol. 234, pp. 113-120, 1992.
Gysler et al., Gene, vol. 89, pp. 101-108, 1990.
Alana et al, FEBS, vol. 280, No. 2, pp. 335-340, 1991.
Harmsen et al. "Cloning and Expression of a second Asp. niger . . . ", Curr. Genet., 18, 161-166, 1990.
Someren et al. "Structure of Asp. niger pelA gene and its exp. . . . ", Curr. Genet., 20, 293-299, 1991.
Gibriel et al. "Level of polygalacturonase, pectin estrase, pectin . . . ", Egypt J. Microbio, 189-198, 1983.
Andersen Lene Nonboe
Christgau Stephan
Dalb.o slashed.ge Henrik
Heldt-Hansen Hans Peter
Kauppinen Markus Sakari
Gregg, Esq. Valeta
Nashed Nashaat T.
Novo Nordisk A S
Wax Robert A.
Zelson Esq. Steve T.
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