Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme

Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a...
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Autor*in:	Suykerbuyk, M. E. G. [verfasserIn] Schaap, P. J. Stam, H. Musters, W. Visser, J.

Format:	Artikel
Sprache:	Englisch

Erschienen:	1995

Schlagwörter:	Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin

Anmerkung:	© Springer-Verlag 1995

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 43(1995), 5 vom: Okt., Seite 861-870
Übergeordnetes Werk:	volume:43 ; year:1995 ; number:5 ; month:10 ; pages:861-870

Links:	Volltext

DOI / URN:	10.1007/BF02431920

Katalog-ID:	OLC2050675453

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245	1	0	\|a Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme
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520			\|a Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process.
650		4	\|a Pectin
650		4	\|a Aspergillus Niger
650		4	\|a Culture Filtrate
650		4	\|a Pectinolytic Enzyme
650		4	\|a Apple Pectin
700	1		\|a Schaap, P. J. \|4 aut
700	1		\|a Stam, H. \|4 aut
700	1		\|a Musters, W. \|4 aut
700	1		\|a Visser, J. \|4 aut
773	0	8	\|i Enthalten in \|t Applied microbiology and biotechnology \|d Springer-Verlag, 1984 \|g 43(1995), 5 vom: Okt., Seite 861-870 \|w (DE-627)129942634 \|w (DE-600)392453-1 \|w (DE-576)015507750 \|x 0175-7598 \|7 nnns
773	1	8	\|g volume:43 \|g year:1995 \|g number:5 \|g month:10 \|g pages:861-870
856	4	1	\|u https://doi.org/10.1007/BF02431920 \|z lizenzpflichtig \|3 Volltext
912			\|a GBV_USEFLAG_A
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912			\|a SSG-OLC-CHE
912			\|a SSG-OLC-PHA
912			\|a SSG-OLC-DE-84
912			\|a GBV_ILN_11
912			\|a GBV_ILN_21
912			\|a GBV_ILN_23
912			\|a GBV_ILN_31
912			\|a GBV_ILN_40
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_130
912			\|a GBV_ILN_252
912			\|a GBV_ILN_267
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2016
912			\|a GBV_ILN_2018
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2360
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4028
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4082
912			\|a GBV_ILN_4103
912			\|a GBV_ILN_4219
912			\|a GBV_ILN_4277
912			\|a GBV_ILN_4302
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4310
951			\|a AR
952			\|d 43 \|j 1995 \|e 5 \|c 10 \|h 861-870

Indexfelder

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matchkey_str	article:01757598:1995----::lnnsqecadxrsinfhgncdnfrhmoaatrnsoaprilsc
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allfields	10.1007/BF02431920 doi (DE-627)OLC2050675453 (DE-He213)BF02431920-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Suykerbuyk, M. E. G. verfasserin aut Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1995 Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin Schaap, P. J. aut Stam, H. aut Musters, W. aut Visser, J. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 43(1995), 5 vom: Okt., Seite 861-870 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:43 year:1995 number:5 month:10 pages:861-870 https://doi.org/10.1007/BF02431920 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 43 1995 5 10 861-870
spelling	10.1007/BF02431920 doi (DE-627)OLC2050675453 (DE-He213)BF02431920-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Suykerbuyk, M. E. G. verfasserin aut Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1995 Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin Schaap, P. J. aut Stam, H. aut Musters, W. aut Visser, J. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 43(1995), 5 vom: Okt., Seite 861-870 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:43 year:1995 number:5 month:10 pages:861-870 https://doi.org/10.1007/BF02431920 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 43 1995 5 10 861-870
allfields_unstemmed	10.1007/BF02431920 doi (DE-627)OLC2050675453 (DE-He213)BF02431920-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Suykerbuyk, M. E. G. verfasserin aut Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1995 Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin Schaap, P. J. aut Stam, H. aut Musters, W. aut Visser, J. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 43(1995), 5 vom: Okt., Seite 861-870 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:43 year:1995 number:5 month:10 pages:861-870 https://doi.org/10.1007/BF02431920 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 43 1995 5 10 861-870
allfieldsGer	10.1007/BF02431920 doi (DE-627)OLC2050675453 (DE-He213)BF02431920-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Suykerbuyk, M. E. G. verfasserin aut Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1995 Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin Schaap, P. J. aut Stam, H. aut Musters, W. aut Visser, J. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 43(1995), 5 vom: Okt., Seite 861-870 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:43 year:1995 number:5 month:10 pages:861-870 https://doi.org/10.1007/BF02431920 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 43 1995 5 10 861-870
allfieldsSound	10.1007/BF02431920 doi (DE-627)OLC2050675453 (DE-He213)BF02431920-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Suykerbuyk, M. E. G. verfasserin aut Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1995 Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin Schaap, P. J. aut Stam, H. aut Musters, W. aut Visser, J. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 43(1995), 5 vom: Okt., Seite 861-870 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:43 year:1995 number:5 month:10 pages:861-870 https://doi.org/10.1007/BF02431920 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 43 1995 5 10 861-870
language	English
source	Enthalten in Applied microbiology and biotechnology 43(1995), 5 vom: Okt., Seite 861-870 volume:43 year:1995 number:5 month:10 pages:861-870
sourceStr	Enthalten in Applied microbiology and biotechnology 43(1995), 5 vom: Okt., Seite 861-870 volume:43 year:1995 number:5 month:10 pages:861-870
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin
dewey-raw	570
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container_title	Applied microbiology and biotechnology
authorswithroles_txt_mv	Suykerbuyk, M. E. G. @@aut@@ Schaap, P. J. @@aut@@ Stam, H. @@aut@@ Musters, W. @@aut@@ Visser, J. @@aut@@
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E. G.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1995</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer-Verlag 1995</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. 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author	Suykerbuyk, M. E. G.
spellingShingle	Suykerbuyk, M. E. G. ddc 570 ssgn 12 fid BIODIV misc Pectin misc Aspergillus Niger misc Culture Filtrate misc Pectinolytic Enzyme misc Apple Pectin Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme
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topic_title	570 VZ 12 ssgn BIODIV DE-30 fid Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme Pectin Aspergillus Niger Culture Filtrate Pectinolytic Enzyme Apple Pectin
topic	ddc 570 ssgn 12 fid BIODIV misc Pectin misc Aspergillus Niger misc Culture Filtrate misc Pectinolytic Enzyme misc Apple Pectin
topic_unstemmed	ddc 570 ssgn 12 fid BIODIV misc Pectin misc Aspergillus Niger misc Culture Filtrate misc Pectinolytic Enzyme misc Apple Pectin
topic_browse	ddc 570 ssgn 12 fid BIODIV misc Pectin misc Aspergillus Niger misc Culture Filtrate misc Pectinolytic Enzyme misc Apple Pectin
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title	Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme
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title_full	Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme
author_sort	Suykerbuyk, M. E. G.
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doi_str_mv	10.1007/BF02431920
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title_sort	cloning, sequence and expression of the gene coding for rhamnogalacturonase ofaspergillus aculeatus; a novel pectinolytic enzyme
title_auth	Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme
abstract	Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. © Springer-Verlag 1995
abstractGer	Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. © Springer-Verlag 1995
abstract_unstemmed	Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process. © Springer-Verlag 1995
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title_short	Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme
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Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme

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