LIVIVO - Search results -

Search results

Result 1 - 9 of total 9

Search options

Article: Active and synchronous control of nitrogen and organic matter release from sediments induced with calcium peroxide

Wang, Wen-Huai / Wang, Yi / Zhao, Ke-Xin / Zhu, Zheng / Han, Xue-Yi

Science of the total environment. 2022 Jan. 01, v. 802

2022

Abstract: In order to realize the active and synchronous control of nitrogen (N) and organic matter (OM) release from sediments, this study compared the spatiotemporal changes in the physical, chemical, and biological indicators in the water system under different ...

Abstract	In order to realize the active and synchronous control of nitrogen (N) and organic matter (OM) release from sediments, this study compared the spatiotemporal changes in the physical, chemical, and biological indicators in the water system under different CaO₂ dosing modes. Results from 90-day incubation experiment showed that CaO₂ formed a dense barrier layer near its dosing position, improved the anoxic condition of water system, increased the physical adsorption of pollutants by sediments, and reduced the nutrients in overlying water, interstitial water, and sediments. Comprehensive comparison, the improvement effect of shallow injection group (I1) was the most obvious. Meanwhile, the activities of ammonia oxidizing bacteria and nitrite oxidizing bacteria near dosing position and those of denitrifiers and anammox bacteria adjacent to dosing site were significantly increased in all test groups (p < 0.01), thereby realizing the biological removal of N and OM in sediments. In addition, DO and ORP were steadily higher than 5 mg L⁻¹ and 100 mV in I1, where the NH₄⁺-N concentration in overlying water was stable below 1 mg L⁻¹, and the easily released N content in the upper (0–3 cm) and middle (4–6 cm) sediments decreased by 41.64% and 43.56%, respectively. Compared with the large pollutant flux in control (14.31 TN mg m⁻² d⁻¹ and 194.05 mg TCOD m⁻² d⁻¹), I1 completely inhibited the pollutant release and reduced the original nutrients in overlying water. In general, CaO₂ efficiently and synchronously controlled the endogenous release of N and OM under the combined actions of physical interception, physical adsorption, chemical oxidation, and biological transformation. Therefore, this study may provide valuable reference and guidance for the active and synchronous removal of N and OM in sediments and inhibition of endogenous pollutant release under anoxic condition.
Keywords	adsorption ; ammonia ; anaerobic ammonium oxidation ; calcium peroxide ; denitrifying microorganisms ; environment ; nitrites ; nitrogen ; organic matter ; oxidation ; pollutants
Language	English
Dates of publication	2022-0101
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	121506-1
ISSN	1879-1026 ; 0048-9697
ISSN (online)	1879-1026
ISSN	0048-9697
DOI	10.1016/j.scitotenv.2021.149855
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 74/341: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Active and synchronous control of nitrogen and organic matter release from sediments induced with calcium peroxide.

Wang, Wen-Huai / Wang, Yi / Zhao, Ke-Xin / Zhu, Zheng / Han, Xue-Yi

The Science of the total environment

2021 Volume 802, Page(s) 149855

Abstract	In order to realize the active and synchronous control of nitrogen (N) and organic matter (OM) release from sediments, this study compared the spatiotemporal changes in the physical, chemical, and biological indicators in the water system under different CaO
MeSH term(s)	Geologic Sediments ; Nitrogen/analysis ; Peroxides ; Phosphorus ; Water Pollutants, Chemical/analysis
Chemical Substances	Peroxides ; Water Pollutants, Chemical ; Phosphorus (27YLU75U4W) ; calcium peroxide (7FRO2ENO91) ; Nitrogen (N762921K75)
Language	English
Publishing date	2021-08-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	121506-1
ISSN	1879-1026 ; 0048-9697
ISSN (online)	1879-1026
ISSN	0048-9697
DOI	10.1016/j.scitotenv.2021.149855
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 949: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Strengthen the purification of eutrophic water and improve the characteristics of sediment by functional ecological floating bed suspended calcium peroxide and sponge iron jointly.

Zhu, Zheng / Wang, Yi / Han, Xue-Yi / Wang, Wen-Huai / Li, Hao-Min / Yue, Zi-Qi / Chen, Wei / Xue, Fu-Rong

Journal of environmental management

2022 Volume 325, Issue Pt B, Page(s) 116610

Abstract: To overcome the shortcomings of conventional ecological floating bed (CEFB) in purifying landscape water, this study constructed a functional ecological floating bed (FEFB) through the suspension of calcium peroxide (CP) and sponge iron (SI) jointly ... ...

Abstract	To overcome the shortcomings of conventional ecological floating bed (CEFB) in purifying landscape water, this study constructed a functional ecological floating bed (FEFB) through the suspension of calcium peroxide (CP) and sponge iron (SI) jointly below the CEFB. The purification effect of water quality and influence of sediment were compared in control check, CEFB, and FEFB systems, which were loaded the same sediment and reclaimed water in a field experiment. Results showed that the FEFB suspended with CP and SI had evident purification effect on the quality of landscape water supplied with reclaimed water and can maintain stably the nutrient status of the water body at mesotrophic levels and low turbidity. The FEFB promoted the degradation of humus, thus eliminating the chroma risk in water body caused by the decay of plants from the CEFB. Moreover, the FEFB can control the sediment mass produced, reduce the total nitrogen (TN) mass of sediment, and decrease the transformable TN (TTN) content in the sediment. The FEFB enhanced the stability of phosphorus (P) in the sediment, where the relative content of Ca-P and stable P reached 42.18% and 64.27%, respectively. To sum up, the FEFB suspended with SI and CP can not only effectively control the eutrophication and sensory index of landscape water but also change the TTN content and P forms in sediment, making the sediment more stable. Thus, the FEFB provides an innovative approach to reduce endogenous nutrient release for landscape water along with recharging with reclaimed water.
MeSH term(s)	Iron ; Phosphorus ; Eutrophication ; Nitrogen/analysis ; Water Pollutants, Chemical/analysis ; Geologic Sediments
Chemical Substances	calcium peroxide (7FRO2ENO91) ; Iron (E1UOL152H7) ; Phosphorus (27YLU75U4W) ; Nitrogen (N762921K75) ; Water Pollutants, Chemical
Language	English
Publishing date	2022-10-31
Publishing country	England
Document type	Journal Article
ZDB-ID	184882-3
ISSN	1095-8630 ; 0301-4797
ISSN (online)	1095-8630
ISSN	0301-4797
DOI	10.1016/j.jenvman.2022.116610
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 7556: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article: Site-Directed Mutagenesis Improves the Thermostability and Catalytic Efficiency of Aspergillus niger N25 Phytase Mutated by I44E and T252R

Liao, Yan / Li, Chun-mei / Chen, Hui / Wu, Qi / Shan, Zhi / Han, Xue-yi

Applied biochemistry and biotechnology. 2013 Oct., v. 171, no. 4

2013

Abstract: Aspergillus niger phytase (PhyA) has been used as a feed supplement to improve the bioavailability of phytate phosphorus to swine and poultry. However, it is unable to maintain its stability due to high temperature during the feed pelleting process. In ... ...

Abstract	Aspergillus niger phytase (PhyA) has been used as a feed supplement to improve the bioavailability of phytate phosphorus to swine and poultry. However, it is unable to maintain its stability due to high temperature during the feed pelleting process. In this study, we performed site-directed mutagenesis in the Aspergillus niger N25 phyA ᵐ gene at residue 44I and 252� T, and they were replaced by glutamic acid and arginine. Single-site mutants I44E-PhyA and T252R-PhyA, as well as double-site mutant I44E/T252R-PhyA, were constructed to improve the thermostability of PhyA through hydrogen bondings and ionic interactions. The three mutant enzymes all showed more than 20� % improvement in thermostability compared to the wild-type enzyme after being heated at 80� °C for 10� min. Their melting temperatures (T ₘ) were increased by 1, 1, and 1.2� °C, respectively. The k ₘ values of I44E-PhyA, T252R-PhyA, and I44E/T252R-PhyA for sodium phytate were 78, 44, and 79� % lower (P <0.05) than that of the wild-type enzyme. Overall catalytic efficiency (k cₐₜ/k ₘ) of I44E-PhyA, T252R-PhyA, and I44E/T252R-PhyA was improved by 310, 155, and 84� % (P <0.05) than that of the wild type, respectively. The catalytic efficiency did not seem to be negatively affected by the improvement in thermostability.
Keywords	Aspergillus niger ; bioavailability ; feed supplements ; genes ; glutamic acid ; hydrogen bonding ; melting point ; mutants ; pelleted feeds ; phosphorus ; phytases ; phytic acid ; poultry ; site-directed mutagenesis ; sodium ; swine ; temperature ; thermal stability
Language	English
Dates of publication	2013-10
Size	p. 900-915.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	392344-7
ISSN	0273-2289
ISSN	0273-2289
DOI	10.1007/s12010-013-0380-2
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 80/718: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Site-directed mutagenesis improves the thermostability and catalytic efficiency of Aspergillus niger N25 phytase mutated by I44E and T252R.

Liao, Yan / Li, Chun-Mei / Chen, Hui / Wu, Qi / Shan, Zhi / Han, Xue-Yi

Applied biochemistry and biotechnology

2013 Volume 171, Issue 4, Page(s) 900–915

Abstract	Aspergillus niger phytase (PhyA) has been used as a feed supplement to improve the bioavailability of phytate phosphorus to swine and poultry. However, it is unable to maintain its stability due to high temperature during the feed pelleting process. In this study, we performed site-directed mutagenesis in the Aspergillus niger N25 phyA (m) gene at residue 44I and 252 T, and they were replaced by glutamic acid and arginine. Single-site mutants I44E-PhyA and T252R-PhyA, as well as double-site mutant I44E/T252R-PhyA, were constructed to improve the thermostability of PhyA through hydrogen bondings and ionic interactions. The three mutant enzymes all showed more than 20 % improvement in thermostability compared to the wild-type enzyme after being heated at 80 °C for 10 min. Their melting temperatures (T m) were increased by 1, 1, and 1.2 °C, respectively. The k m values of I44E-PhyA, T252R-PhyA, and I44E/T252R-PhyA for sodium phytate were 78, 44, and 79 % lower (P <0.05) than that of the wild-type enzyme. Overall catalytic efficiency (k cat/k m) of I44E-PhyA, T252R-PhyA, and I44E/T252R-PhyA was improved by 310, 155, and 84 % (P <0.05) than that of the wild type, respectively. The catalytic efficiency did not seem to be negatively affected by the improvement in thermostability.
MeSH term(s)	6-Phytase/chemistry ; 6-Phytase/genetics ; 6-Phytase/metabolism ; Aspergillus niger/enzymology ; Enzyme Stability ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Mutagenesis, Site-Directed/methods ; Temperature
Chemical Substances	Fungal Proteins ; 6-Phytase (EC 3.1.3.26)
Language	English
Publishing date	2013-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392344-7
ISSN	1559-0291 ; 0273-2289
ISSN (online)	1559-0291
ISSN	0273-2289
DOI	10.1007/s12010-013-0380-2
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 3053: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: An antifungal peptide from Fagopyrum tataricum seeds.

Ruan, Jing-Jun / Chen, Hui / Shao, Ji-Rong / Wu, Qi / Han, Xue-Yi

Peptides

2011 Volume 32, Issue 6, Page(s) 1151–1158

Abstract: A major trypsin inhibitor was isolated and characterized from the seeds of the tartary buckwheat (Fagopyrum tataricum) (FtTI) by ammonium sulfate precipitation, ion exchange chromatography and centrifugal ultrafiltration. SDS-PAGE analysis under reducing ...

Abstract	A major trypsin inhibitor was isolated and characterized from the seeds of the tartary buckwheat (Fagopyrum tataricum) (FtTI) by ammonium sulfate precipitation, ion exchange chromatography and centrifugal ultrafiltration. SDS-PAGE analysis under reducing condition showed that FtTI is a single polypeptide chain with a molecular mass of approximately 14kDa. The complete amino acid sequence of FtTI was established by automatic Edman degradation and mass spectrometry. It was found that the trypsin inhibitor molecule consists of 86 amino acid residues containing two disulfide bonds which connect Cys(8) to Cys(65) and Cys(49) to Cys(58). The active site of the inhibitor was found to contain an Asp(66)-Arg(67) bond. MALDI-TOF analysis showed that FtTI has two isoforms (Mr: 11.487 and 13.838kDa). Dixon plots revealed a competitive inhibition of trypsin with inhibition constants (Ki) of 1.6nM. Analysis of the amino acid sequence suggests that FtTI is a member of the protease inhibitor I family. What is more, FtTI exhibited strong inhibitory activity against phytopathogenic fungi.
MeSH term(s)	Amino Acid Sequence ; Antifungal Agents/chemistry ; Antifungal Agents/isolation & purification ; Antifungal Agents/metabolism ; Antifungal Agents/pharmacology ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Fagopyrum/chemistry ; Fagopyrum/metabolism ; Fungi/drug effects ; Fungi/growth & development ; Mass Spectrometry ; Molecular Sequence Data ; Phylogeny ; Plant Diseases/microbiology ; Plant Proteins/chemistry ; Plant Proteins/isolation & purification ; Plant Proteins/metabolism ; Plant Proteins/pharmacology ; Protein Isoforms/chemistry ; Protein Isoforms/isolation & purification ; Protein Isoforms/metabolism ; Protein Isoforms/pharmacology ; Seeds/chemistry ; Seeds/metabolism ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Trypsin/metabolism ; Trypsin Inhibitors/chemistry ; Trypsin Inhibitors/isolation & purification ; Trypsin Inhibitors/metabolism ; Trypsin Inhibitors/pharmacology ; Ultrafiltration
Chemical Substances	Antifungal Agents ; Plant Proteins ; Protein Isoforms ; Trypsin Inhibitors ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2011-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	769028-9
ISSN	1873-5169 ; 0196-9781
ISSN (online)	1873-5169
ISSN	0196-9781
DOI	10.1016/j.peptides.2011.03.015
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1649: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Improving phytase enzyme activity in a recombinant phyA mutant phytase from Aspergillus niger N25 by error-prone PCR.

Liao, Yan / Zeng, Min / Wu, Zhen-Fang / Chen, Hui / Wang, Hong-Ning / Wu, Qi / Shan, Zhi / Han, Xue-Yi

Applied biochemistry and biotechnology

2012 Volume 166, Issue 3, Page(s) 549–562

Abstract: The mutant acid phytase (phyA ( m )) gene was modified by random mutagenesis to improve enzymatic activity by using an error-prone PCR (ep-PCR) strategy. The mutated gene was linearized and inserted into plasmid vector pPIC9K and transformed by ... ...

Abstract	The mutant acid phytase (phyA ( m )) gene was modified by random mutagenesis to improve enzymatic activity by using an error-prone PCR (ep-PCR) strategy. The mutated gene was linearized and inserted into plasmid vector pPIC9K and transformed by electroporation into Pichia pastoris GS115. A single transformant, PP-NP(ep)-6A, showing the strongest phytase activity from among the 5,500 transformants, was selected for detailed analyses. Southern blot analysis of the mutant yeast transformant showed that phyA ( ep ) gene was integrated into the chromosome genome through single crossover with one copy of phyA. The kinetic parameters indicated that the mutant one showed 61% higher specific activity and 53% lower k (m) value than that of PP-NP(m)-8 (P < 0.05). In addition, the overall catalytic efficiency (k (cat)/k (m)) of the mutant one was 84% higher (P < 0.05) than that of PP-NP(m)-8. Nine bases were altered in the mutant sequences, which resulted in three amino acid changes, namely, Glu156Gly, Thr236Ala, and Gln396Arg. The structural predictions indicated that the mutations generated by ep-PCR somehow reorganized or remodeled the active site, which could lead to increasing catalytic efficiency.
MeSH term(s)	6-Phytase/chemistry ; 6-Phytase/genetics ; 6-Phytase/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Aspergillus niger/enzymology ; Aspergillus niger/genetics ; Biocatalysis ; Catalytic Domain ; Electroporation ; Escherichia coli ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Genome, Fungal ; Genomic Library ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Pichia/enzymology ; Pichia/genetics ; Polymerase Chain Reaction ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Substrate Specificity
Chemical Substances	Fungal Proteins ; Recombinant Proteins ; 6-Phytase (EC 3.1.3.26)
Language	English
Publishing date	2012-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392344-7
ISSN	1559-0291 ; 0273-2289
ISSN (online)	1559-0291
ISSN	0273-2289
DOI	10.1007/s12010-011-9447-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 3053: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Improving Phytase Enzyme Activity in a Recombinant phyA Mutant Phytase from Aspergillus niger N25 by Error-Prone PCR

Liao, Yan / Zeng, Min / Wu, Zhen-fang / Chen, Hui / Wang, Hong-ning / Wu, Qi / Shan, Zhi / Han, Xue-yi

Applied biochemistry and biotechnology. 2012 Feb., v. 166, no. 3

2012

Abstract: The mutant acid phytase (phyA m ) gene was modified by random mutagenesis to improve enzymatic activity by using an error-prone PCR (ep-PCR) strategy. The mutated gene was linearized and inserted into plasmid vector pPIC9K and transformed by ... ...

Abstract	The mutant acid phytase (phyA m ) gene was modified by random mutagenesis to improve enzymatic activity by using an error-prone PCR (ep-PCR) strategy. The mutated gene was linearized and inserted into plasmid vector pPIC9K and transformed by electroporation into Pichia pastoris GS115. A single transformant, PP-NPep-6A, showing the strongest phytase activity from among the 5,500 transformants, was selected for detailed analyses. Southern blot analysis of the mutant yeast transformant showed that phyA ep gene was integrated into the chromosome genome through single crossover with one copy of phyA. The kinetic parameters indicated that the mutant one showed 61% higher specific activity and 53% lower k m value than that of PP-NPm-8 (P < 0.05). In addition, the overall catalytic efficiency (k cat/k m) of the mutant one was 84% higher (P < 0.05) than that of PP-NPm-8. Nine bases were altered in the mutant sequences, which resulted in three amino acid changes, namely, Glu156Gly, Thr236Ala, and Gln396Arg. The structural predictions indicated that the mutations generated by ep-PCR somehow reorganized or remodeled the active site, which could lead to increasing catalytic efficiency.
Keywords	Aspergillus niger ; Pichia pastoris ; Southern blotting ; active sites ; amino acids ; chromosomes ; electroporation ; enzyme activity ; genes ; mutants ; mutation ; phytases ; plasmid vectors ; polymerase chain reaction ; prediction ; recombinant proteins ; yeasts
Language	English
Dates of publication	2012-02
Size	p. 549-562.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	392344-7
ISSN	0273-2289
ISSN	0273-2289
DOI	10.1007/s12010-011-9447-0
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 80/718: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article: antifungal peptide from Fagopyrum tataricum seeds

Ruan, Jing-Jun / Chen, Hui / Shao, Ji-Rong / Wu, Qi / Han, Xue-Yi

Peptides

Volume v. 32,, Issue no. 6

Abstract	A major trypsin inhibitor was isolated and characterized from the seeds of the tartary buckwheat (Fagopyrum tataricum) (FtTI) by ammonium sulfate precipitation, ion exchange chromatography and centrifugal ultrafiltration. SDS-PAGE analysis under reducing condition showed that FtTI is a single polypeptide chain with a molecular mass of approximately 14kDa. The complete amino acid sequence of FtTI was established by automatic Edman degradation and mass spectrometry. It was found that the trypsin inhibitor molecule consists of 86 amino acid residues containing two disulfide bonds which connect Cys⁸ to Cys⁶⁵ and Cys⁴⁹ to Cys⁵⁸. The active site of the inhibitor was found to contain an Asp⁶⁶–Arg⁶⁷ bond. MALDI-TOF analysis showed that FtTI has two isoforms (Mr: 11.487 and 13.838kDa). Dixon plots revealed a competitive inhibition of trypsin with inhibition constants (Ki) of 1.6nM. Analysis of the amino acid sequence suggests that FtTI is a member of the protease inhibitor I family. What is more, FtTI exhibited strong inhibitory activity against phytopathogenic fungi.
Keywords	Fagopyrum tataricum ; amino acid composition ; amino acid sequences ; molecular weight ; active sites ; polypeptides ; buckwheat ; trypsin ; plant pathogenic fungi ; disulfide bonds ; ammonium sulfate ; ion exchange chromatography ; mass spectrometry ; amino acids ; trypsin inhibitors ; seeds ; ultrafiltration ; antimicrobial peptides ; polyacrylamide gel electrophoresis
Language	English
Document type	Article
ISSN	0196-9781
Database	AGRIS - International Information System for the Agricultural Sciences and Technology

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

Your last searches

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED