@article{HagerHentschkeHojdisetal.2015,
  author    = {Hager, Jonathan and Hentschke, Reinhard and Hojdis, Nils and Karimi-Varzaneh, Hossein Ali},
  title     = {Computer Simulation of Particle-Particle Interaction in a Model Polymer Nanocomposite},
  series = {Macromolecules},
  volume    = {48},
  journal   = {Macromolecules},
  number    = {24},
  issn      = {1520-5835},
  doi       = {10.1021/acs.macromol.5b01864},
  pages     = {9039 -- 9049},
  year      = {2015},
  language  = {en}
}
@article{HafidiElHatkaSchmitzetal.2024,
  author    = {Hafidi, Youssef and El Hatka, Hicham and Schmitz, Dominik and Krauss, Manuel and Pettrak, J{\"u}rgen and Biel, Markus and Ittobane, Najim},
  title     = {Sustainable soil additives for water and micronutrient supply: swelling and chelating properties of polyaspartic acid hydrogels utilizing newly developed crosslinkers},
  series = {Gels},
  volume    = {10},
  journal   = {Gels},
  number    = {3},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2310-2861},
  doi       = {10.3390/gels10030170},
  pages     = {Artikel 170},
  year      = {2024},
  abstract  = {Drought and water shortage are serious problems in many arid and semi-arid regions. This problem is getting worse and even continues in temperate climatic regions due to climate change. To address this problem, the use of biodegradable hydrogels is increasingly important for the application as water-retaining additives in soil. Furthermore, efficient (micro-)nutrient supply can be provided by the use of tailored hydrogels. Biodegradable polyaspartic acid (PASP) hydrogels with different available (1,6-hexamethylene diamine (HMD) and L-lysine (LYS)) and newly developed crosslinkers based on diesters of glycine (GLY) and (di-)ethylene glycol (DEG and EG, respectively) were synthesized and characterized using Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) and regarding their swelling properties (kinetic, absorbency under load (AUL)) as well as biodegradability of PASP hydrogel. Copper (II) and zinc (II), respectively, were loaded as micronutrients in two different approaches: in situ with crosslinking and subsequent loading of prepared hydrogels. The results showed successful syntheses of di-glycine-ester-based crosslinkers. Hydrogels with good water-absorbing properties were formed. Moreover, the developed crosslinking agents in combination with the specific reaction conditions resulted in higher water absorbency with increased crosslinker content used in synthesis (10\% vs. 20\%). The prepared hydrogels are candidates for water-storing soil additives due to the biodegradability of PASP, which is shown in an exemple. The incorporation of Cu(II) and Zn(II) ions can provide these micronutrients for plant growth.},
  language  = {en}
}
@article{HaegerProbstJaegeretal.2023,
  author    = {Haeger, Gerrit and Probst, Johanna and Jaeger, Karl-Erich and Bongaerts, Johannes and Siegert, Petra},
  title     = {Novel aminoacylases from Streptomyces griseus DSM 40236 and their recombinant production in Streptomyces lividans},
  series = {FEBS Open Bio},
  volume    = {13},
  journal   = {FEBS Open Bio},
  number    = {12},
  publisher = {Wiley},
  address   = {Hoboken, NJ},
  issn      = {2211-5463},
  doi       = {10.1002/2211-5463.13723},
  pages     = {2224 -- 2238},
  year      = {2023},
  abstract  = {Amino acid-based surfactants are valuable compounds for cosmetic formulations. The chemical synthesis of acyl-amino acids is conventionally performed by the Schotten-Baumann reaction using fatty acyl chlorides, but aminoacylases have also been investigated for use in biocatalytic synthesis with free fatty acids. Aminoacylases and their properties are diverse; they belong to different peptidase families and show differences in substrate specificity and biocatalytic potential. Bacterial aminoacylases capable of synthesis have been isolated from Burkholderia, Mycolicibacterium, and Streptomyces. Although several proteases and peptidases from S. griseus have been described, no aminoacylases from this species have been identified yet. In this study, we investigated two novel enzymes produced by S. griseus DSM 40236ᵀ . We identified and cloned the respective genes and recombinantly expressed an α-aminoacylase (EC 3.5.1.14), designated SgAA, and an ε-lysine acylase (EC 3.5.1.17), designated SgELA, in S. lividans TK23. The purified aminoacylase SgAA was biochemically characterized, focusing on its hydrolytic activity to determine temperature- and pH optima and stabilities. The aminoacylase could hydrolyze various acetyl-amino acids at the Nα -position with a broad specificity regarding the sidechain. Substrates with longer acyl chains, like lauroyl-amino acids, were hydrolyzed to a lesser extent. Purified aminoacylase SgELA specific for the hydrolysis of Nε -acetyl-L-lysine was unstable and lost its enzymatic activity upon storage for a longer period but could initially be characterized. The pH optimum of SgELA was pH 8.0. While synthesis of acyl-amino acids was not observed with SgELA, SgAA catalyzed the synthesis of lauroyl-methionine.},
  language  = {en}
}
@article{HaegerGrankinWagner2023,
  author    = {Haeger, Gerrit and Grankin, Alina and Wagner, Michaela},
  title     = {Construction of an Aspergillus oryzae triple amylase deletion mutant as a chassis to evaluate industrially relevant amylases using multiplex CRISPR/Cas9 editing technology},
  series = {Applied Research},
  journal   = {Applied Research},
  number    = {Early View},
  publisher = {Wiley-VCH},
  issn      = {2702-4288},
  doi       = {10.1002/appl.202200106},
  pages     = {1 -- 15},
  year      = {2023},
  abstract  = {Aspergillus oryzae is an industrially relevant organism for the secretory production of heterologous enzymes, especially amylases. The activities of potential heterologous amylases, however, cannot be quantified directly from the supernatant due to the high background activity of native α-amylase. This activity is caused by the gene products of amyA, amyB, and amyC. In this study, an in vitro CRISPR/Cas9 system was established in A. oryzae to delete these genes simultaneously. First, pyrG of A. oryzae NSAR1 was mutated by exploiting NHEJ to generate a counter-selection marker. Next, all amylase genes were deleted simultaneously by co-transforming a repair template carrying pyrG of Aspergillus nidulans and flanking sequences of amylase gene loci. The rate of obtained triple knock-outs was 47\%. We showed that triple knockouts do not retain any amylase activity in the supernatant. The established in vitro CRISPR/Cas9 system was used to achieve sequence-specific knock-in of target genes. The system was intended to incorporate a single copy of the gene of interest into the desired host for the development of screening methods. Therefore, an integration cassette for the heterologous Fpi amylase was designed to specifically target the amyB locus. The site-specific integration rate of the plasmid was 78\%, with exceptional additional integrations. Integration frequency was assessed via qPCR and directly correlated with heterologous amylase activity. Hence, we could compare the efficiency between two different signal peptides. In summary, we present a strategy to exploit CRISPR/Cas9 for gene mutation, multiplex knock-out, and the targeted knock-in of an expression cassette in A. oryzae. Our system provides straightforward strain engineering and paves the way for development of fungal screening systems.},
  language  = {en}
}
@article{HaegerBongaertsSiegert2022,
  author    = {Haeger, Gerrit and Bongaerts, Johannes and Siegert, Petra},
  title     = {A convenient ninhydrin assay in 96-well format for amino acid-releasing enzymes using an air-stable reagent},
  series = {Analytical Biochemistry},
  journal   = {Analytical Biochemistry},
  number    = {624},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1096-0309},
  doi       = {10.1016/j.ab.2022.114819},
  pages     = {Artikel 114819},
  year      = {2022},
  abstract  = {An improved and convenient ninhydrin assay for aminoacylase activity measurements was developed using the commercial EZ Nin™ reagent. Alternative reagents from literature were also evaluated and compared. The addition of DMSO to the reagent enhanced the solubility of Ruhemann's purple (RP). Furthermore, we found that the use of a basic, aqueous buffer enhances stability of RP. An acidic protocol for the quantification of lysine was developed by addition of glacial acetic acid. The assay allows for parallel processing in a 96-well format with measurements microtiter plates.},
  language  = {en}
}
@article{GuoMiyamotoWagneretal.2014,
  author    = {Guo, Yuanyuan and Miyamoto, Ko-ichiro and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo},
  title     = {Theoretical study and simulation of light-addressable potentiometric sensors},
  series = {Physica status solidi (A) : applications and materials},
  volume    = {211},
  journal   = {Physica status solidi (A) : applications and materials},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0031-8965},
  doi       = {10.1002/pssa.201330354},
  pages     = {1467 -- 1472},
  year      = {2014},
  abstract  = {The light-addressable potentiometric sensor (LAPS) is a semiconductor-based potentiometric sensor using a light probe with an ability of detecting the concentration of biochemical species in a spatially resolved manner. As an important biomedical sensor, research has been conducted to improve its performance, for instance, to realize high-speed measurement. In this work, the idea of facilitating the device-level simulation, instead of using an equivalent-circuit model, is presented for detailed analysis and optimization of the performance of the LAPS. Both carrier distribution and photocurrent response have been simulated to provide new insight into both amplitude-mode and phase-mode operations of the LAPS. Various device parameters can be examined to effectively design and optimize the LAPS structures and setups for enhanced performance.},
  language  = {en}
}
@article{GrafSteinhofLotzetal.2009,
  author    = {Graf, Alain-Michel and Steinhof, Rafael and Lotz, Martin and Tippk{\"o}tter, Nils and Kasper, Cornelia and Beutel, Sascha and Ulber, Roland},
  title     = {Downstream-Processing mit Membranadsorbern zur Isolierung nativer Proteinfraktionen aus Kartoffelfruchtwasser},
  series = {Chemie Ingenieur Technik},
  volume    = {81},
  journal   = {Chemie Ingenieur Technik},
  number    = {3},
  publisher = {Wiley},
  address   = {Weinheim},
  doi       = {10.1002/cite.200800139},
  pages     = {267 -- 274},
  year      = {2009},
  abstract  = {Bei der St{\"a}rkeproduktion entstehendes Kartoffelfruchtwasser besitzt mit 2 - 3 \% einen hohen Anteil an ern{\"a}hrungsphysiologisch interessanten Proteinen. Die industrielle Gewinnung dieser Proteinfracht liefert jedoch lediglich ein minderwertiges, denaturiertes Produkt. Mit Hilfe der Membranadsorber-Technologie lassen sich aus Kartoffelfruchtwasser unter milden Reaktionsbedingungen native bioaktive Proteinfraktionen gewinnen. Geeignete Trennbedingungen wurden im Labormaßstab entwickelt und in den Technikumsmaßstab {\"u}bertragen. An Anionenaustauscher-Membranadsorbern mit einer Membranfl{\"a}che von 10 000 cm2 wurde eine Patatinhaltige Fraktion (44 kDa) mit Bindungskapazit{\"a}ten von 0,37 mg/cm2 isoliert. Eine niedermolekulare Proteinfraktion mit Protease-Inhibitoren konnte durch Kationenaustauscher-Membranadsorber mit Bindungskapazit{\"a}ten von 1,00 mg/cm2 gewonnen werden. Sie ist f{\"u}r verschiedenste Applikationen in der pharmazeutischen, kosmetischen und der Nahrungsmittelindustrie interessant z. B. f{\"u}r Appetitz{\"u}gler oder muskelaufbauende Proteinpr{\"a}parate. Der Aufreinigung der nativen Proteinfraktionen durch Ultra-/Diafiltration schließt sich die Konfektionierung durch Spr{\"u}htrocknung an. Die bioanalytische Charakterisierung der Produkte belegt die Reinheit und die enzymatische Aktivit{\"a}t sowie die Abreicherung von St{\"o}rkomponenten wie Glykoalkaloide und Polyphenoloxidasen.},
  language  = {de}
}
@article{GoetzeBaerWinkelmannetal.2005,
  author    = {Goetze, Sandra and Baer, Alexandra and Winkelmann, Silke and Nehlsen, Kristina and Seibler, Jost and Maass, Karin and Bode, J{\"u}rgen},
  title     = {Performance of genomic bordering elements at predefined genomic loci},
  series = {Molecular and Cellular Biology},
  volume    = {25},
  journal   = {Molecular and Cellular Biology},
  number    = {6},
  issn      = {1098-5549},
  doi       = {10.1128/MCB.25.6.2260-2272.2005},
  pages     = {2260 -- 2272},
  year      = {2005},
  language  = {en}
}
@article{GlaserLubitzLovelandetal.2009,
  author    = {Glaser, Stefan and Lubitz, Sandra and Loveland, Kate L. and Ohbo, Kazu and Robb, Lorraine and Schwenk, Frieder and Seibler, Jost and Roellig, Daniela and Kranz, Andrea and Anastassiadis, Konstantinos and Stewart, A. Francis},
  title     = {The histone 3 lysine 4 methyltransferase, Mll2, is only required briefly in development and spermatogenesis},
  series = {Epigenetics \& Chromatin},
  volume    = {2},
  journal   = {Epigenetics \& Chromatin},
  number    = {5},
  issn      = {1756-8935},
  doi       = {10.1186/1756-8935-2-5},
  pages     = {1 -- 16},
  year      = {2009},
  language  = {en}
}
@article{GielenWolfBerndtetal.1979,
  author    = {Gielen, Hans-G{\"u}nther and Wolf, G{\"u}nter and Berndt, Heinz and Zahn, Helmut},
  title     = {Synthese der Fragmente A1-8, A9-15 und A16-21 der Schafinsulin-A-Kette unter Verwendung des S-tert-Butylmercaptorestes als Thiolschutzgruppe},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {2},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.2.1535},
  pages     = {1535 -- 1548},
  year      = {1979},
  language  = {de}
}