| | 2 | Author
| ArminH. Ildebrandt, Rudolf Mengel, HelmutW. Sauer | Requires cookie* | | | Title
| Characterization of an Endogenous Transcription Inhibitor from Physarum polycephalum  | | | | Abstract
| A substance has been purified from isolated nuclei of Physarum polycephalum by equilibrium and velocity gradient centrifugations, ion exchange chromatography and gel filtration which has a high molecular weight, can be labeled in vivo with 32P, is heat stable and resistant to amylases, proteases, nucleases and phosphodiesterase but is sensitive to phosphatases or hydrolysis. This material consists of phospate and glycerol. It selectively inhibits in vitro transcription of RNA polymerases, predominantly the homologous enzyme A by binding to the enzyme. In the presence of this inhibitor of transcription a stable RNA polymerase-template complex cannot be formed. Binding to and inactivation of RNA polymerase is reversible at high ionic strength. | | | |
Reference
| Z. Naturforsch. 34c, 76 (1979); received July 3/ November 21 1978 | | | |
Published
| 1979 | | | |
Keywords
| RNA polymerases, Inhibitor, Glycerophosphate, Physarum | | | |
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| | | | | TEI-XML for
| default:Reihe_C/34/ZNC-1979-34c-0076.pdf | | | | Identifier
| ZNC-1979-34c-0076 | | | | Volume
| 34 | |
| 4 | Author
| Magdolna Droppa, Sándor Demeter, Zsuzsa Rózsa, G. Ábor Horváth | Requires cookie* | | | Title
| Reinvestigation of the Effects of Disalicylidenepropanediamine (DSPD) and 2-HeptyM-hydroxyquinoline-N-oxide (HQNO) on Photosynthetic Electron Transport | | | | Abstract
| The effects of disalicylidenepropanediamine (DSPD) and 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO) on photosynthetic electron transport have been reexamined. The results confirm earlier observations that lower concentrations of DSPD (< 100 hm) block electron transport at the levels of ferredoxin and plastocyanin. High concentrations o f DSPD even inhibit electron transport from HaO -> pBQ, suggesting that DSPD has an inhibitory site in PS II as well. Thermoluminescence curves o f DSPD and DCMU treated chloroplasts were very similar, showing that the third inhibitory site o f DSPD is similar to that o f DCMU. Both oxidized and reduced HQNO, (0 .6 -6 hm) blocked electron transport from H20 -* pBQ, H20 -*■ MV/FeCy to a similar extent. The effect of HQNO on thermoluminescence showed that its inhibitory site is probably located before that o f DCMU. At higher concentration (> 6 h m) , the H20 -*■ MV/FeCy reactions were more strongly inhibited by oxidized HQNO than those occuring from H20 -> pBQ, suggesting that a new site o f inhibition must also be considered. The dark decay of the P 700 signal was not influenced by the addition o f oxidized HQNO which shows that the new inhibitory site of HQNO is located between plastoquinone and P 700. The reduced form of HQNO did not inhibit non-cyclic electron transport around PS I. Indeed, at higher concentrations, reduced HQNO even accelerates electron flow from DCIP -» MV and the dark reduction of P 700, thus suggesting that this compound has a "donor-mediator" function in PS I. | | | |
Reference
| Z. Naturforsch. 36c, 109 (1981); received September 8/October 28 1980 | | | |
Published
| 1981 | | | |
Keywords
| Inhibitors, Electron Transport, Chloroplasts, Thermoluminescence | | | |
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| | | | | TEI-XML for
| default:Reihe_C/36/ZNC-1981-36c-0109.pdf | | | | Identifier
| ZNC-1981-36c-0109 | | | | Volume
| 36 | |
| 5 | Author
| A. Trebst, B. D. Epka, S. M. Ridley, A. F. Hawkins | Requires cookie* | | | Title
| Inhibition of Photosynthetic Electron Transport by Halogenated 4-Hydroxy-pyridines | | | | Abstract
| Herbicidal halogen substituted 4-hydroxypyridines are inhibitors of photosynthetic electron flow in isolated thylakoid membranes by interfering with the acceptor side of photosystem II. Tetrabromo-4-hydroxypyridine, the most active compound found, has a pl50-value of 7.6 in the inhibition of oxygen evolution in both the reduction of an acceptor of photosystem I and an acceptor of photosystem II. The new inhibitors displace both metribuzin and ioxynil from the membrane. The 4-hydroxypyridines, like ioxynil, have unimpaired inhibitor potency in Tris-treated chloroplasts, whereas the DCMU-type family of herbicides does not. It is suggested that 4-hydroxypyridines are complementary to phenol-type inhibitors, and a common essential element is proposed. The 4-hydroxypyridines do not inhibit photosystem I or non-cyclic electron flow through the cytochrome b/f complex. But they do have a second inhibition site in photosynthetic electron transport since they inhibit ferredoxin-catalyzed cyclic electron flow, indicating an antimycin-like property. A comparison of the in vitro potency of the compounds with the in vivo potency shows no correlation. A major herbicidal mode of action of the group is related to the inhibition of carotenoid synthesis, and access to the chloroplast lamellae in vivo for inhibition of electron transport may be restricted. | | | |
Reference
| Z. Naturforsch. 40c, 391—399 (1985); received February 28 1985 | | | |
Published
| 1985 | | | |
Keywords
| Herbicides, Hydroxypyridines, Inhibitors, Photosynthesis | | | |
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| | | | | TEI-XML for
| default:Reihe_C/40/ZNC-1985-40c-0391.pdf | | | | Identifier
| ZNC-1985-40c-0391 | | | | Volume
| 40 | |
| 6 | Author
| A. Trebst, E. Harth | Requires cookie* | | | Title
| Herbicidal N-Alkylated-Ureas and Ringclosed N-Acylamides as Inhibitors of Photosystem II | | | | Abstract
| The inhibitory action of some herbicides on photosynthetic electron flow at photosystem I I in isolated chloroplasts was investigated. Emphasis in the study is on compounds, whose chemical structure seemed to be in disaccordance with the basic structural element, proposed to be required for a photosystem II inhibitor. The effective inhibition of photosynthetic oxygen evolution by N-alkylated urea-, pyrrolidone-and by substituted pyridazine-derivatives without a free NH-group is reported. A revised basic chemical structural element responsible for inhibition is deduced in order to include lactames (ringclosed N-acylamides) with and without hetero atoms. From this new groups of potential inhibitors, like triazolone-, thiadiazolone-and oxadiazolone-derivatives may be conceived. | | | |
Reference
| (Z. Naturforsch. 29c, 232 [1974]; received February 4 1974) | | | |
Published
| 1974 | | | |
Keywords
| Inhibitor, Herbicides, Photosynthesis, Photosystem II, Chloroplasts | | | |
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| default:Reihe_C/29/ZNC-1974-29c-0232.pdf | | | | Identifier
| ZNC-1974-29c-0232 | | | | Volume
| 29 | |
| 8 | Author
| A. Trebst, S. R. Eim Er, W. Draber, H. J. Knops | Requires cookie* | | | Title
| The Effect of Analogues of Dibromothymoquinone and of Bromonitrothymol on Photosynthetic Electron Flow | | | | Abstract
| Alkyl substituted derivatives of halogenated p-benzoquinones, of halogenated /7-nitrophenols, and of 2,4-dinitrophenols were tested in the inhibition of photosynthetic electron flow in chloro plasts. The effect of the compounds on photoreductions by photosystem I or II, on a TMPD bypass in NADPH formation and the reversibility of the inhibition by dithiothreitol is used to distin guish between an inhibition site before or after plastoquinone function, i. e. between a DBMIB versus a DCMU inhibition pattern. It is shown, that different isopropyl and /-butyl substituted halogenated p-benzoquinones are as effective and specific as DBMIB in the inhibition of plastoquinone function. Alkyl substituted /^-nitrophenols, with an additional halogen-or nitro-group at C-2, are shown to be effective electron flow inhibitors. The new potent nitrophenol derivatives inhibit at the site of DCMU action, nevertheless they do not contain the basic chemical element essential for inhibi tion common to DCMU and its many herbicidal analogues. Small changes in the ring-substitution can alter the inhibition pattern from a DCMU typ to a DBMIB typ inhibition. | | | |
Reference
| Z. Naturforsch. 34c, 831 (1979); received June 1 1979 | | | |
Published
| 1979 | | | |
Keywords
| Photosynthesis, Inhibitors, Herbicides, Dibromothymoquinone, Nitrophenols, Chloroplast | | | |
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| default:Reihe_C/34/ZNC-1979-34c-0831.pdf | | | | Identifier
| ZNC-1979-34c-0831 | | | | Volume
| 34 | |
| 9 | Author
| Klaus Pfister, CharlesJ. Arntzen | Requires cookie* | | | Title
| The Mode of Action of Photosystem II-Specific Inhibitors in Herbicide-Resistant Weed Biotypes | | | | Abstract
| This report reviews studies which provide evidence defining the mode of action and site of action of photosystem II (PS II) herbicides; the involvement of the secondary electron carrier on the reducing side of PS II (called B) is indicated as the target site for these compounds. These studies of the action of PS II-inhibitors were perform ed in chloroplasts of various weed species in order to define the mechanism which is responsible for herbicide tolerance at the level of chloroplast mem branes in newly discovered triazine-resistant weed biotypes. M any species of triazine-resistant weed biotypes have been collected in N orth America and Europe. W here data is available, these plants have been found to share the following common fe atu res: a) they were discovered in areas where triazine herbicides had been used repeatedly, b) resistance to the triazines is extrem e; it is not due to a m inor shift in herbicidal response, c) no changes in herbicide uptake, translocation or metabolism — as compared to susceptible bio types — can be detected, d) resistance is selective for only certain classes of photosynthetic herbicides, and, e) chloroplasts isolated from triazine-resistant weeds display high preferential resistance to the triazines in assays of photosystem II partial reactions. To focus on the mechanism which regulates preferential herbicide activity, we have characterized susceptible and resistant chloroplasts in the presence and absence of herbicides. Properties of the PS II complex of chloroplasts from several different triazine-resistant weed biotypes share the fol lowing tr a its : a) the herbicide binding site (as measured by direct binding of radiolabeled herbicides or by in hibition experiments) is modified such that the affinity for triazines is dram atically reduced. b) alterations in response to many PS II-herbicides occur such th at the triazine-resistant chloro plasts are very strongly resistant to all sym m etrical triazines, strongly resistant to assymmetrical triazinones, partially resistant to pyridazones and uracils, only slightly resistant to ureas or amides, and increasingly susceptible to nitrophenols, phenols and the herbicide bentazon (all as compared to susceptible chloroplasts), c) there is a change in the reaction kinetics of the electron transport step between the prim ary and secondary electron acceptors (referred to as Q and B), and d) in two examples, specific small changes in a m em brane polypeptide can be detected in the resistant thylakoids. We suggest that certain amino acids or segments of the apoprotein of B (the bound quinone which acts as the secondary electron carrier) are modified or deleted in these chloroplasts. Such a polypeptide change could affect both the redox poising of the Q~/B reaction pair, and the specific binding of herbicides. | | | |
Reference
| Z. Naturforsch. 34c, 996—1009 (1979); received June 29 1979 | | | |
Published
| 1979 | | | |
Keywords
| Herbicide, Resistance, Photosynthesis, Electron Transport, Inhibitors | | | |
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| | | | | TEI-XML for
| default:Reihe_C/34/ZNC-1979-34c-0996.pdf | | | | Identifier
| ZNC-1979-34c-0996 | | | | Volume
| 34 | |
| 10 | Author
| Toshihisa Ohshima, Gerhart Drews | Requires cookie* | | | Title
| Isolation and Partial Characterization of the Membrane-Bound NADH Dehydrogenase from the Phototrophic Bacterium Rhodopseudomonas capsulata | | | | Abstract
| Chem otrophically grown cells of Rhodopseudomonas capsulata contain at least three different pyridine nucleotide dehydrogenases, i) a soluble, found in the supernatant (144000 x g) o f cell free extracts, N AD H-dependent, ii) a mem brane-bound, N AD H -dependent, and iii) a soluble, found in the supernatant N AD PH dependent. i The m em brane-bound N A D H dehydrogenase (E.C. 1.6.99.3) has been solubilized by sodium deoxycholate treatm ent of m em branes and purified 75 fold by column chrom atography on Sephadex G-150 and DEAE cellulose in the presence of sodium cholate. The native enzyme has an apparent molecular mass (M r) o f 97 000, containing polypeptides of Mr of about 15 000. The pH optim um was at 7.5. The enzyme was specific for NADH. The Michaelis constant for NADH and DCIP were 4.0 and 63 hm, respectively. The enzyme was inactivated by FM N, riboflavin and NADH. In contrast, the soluble N ADH-dehydrogenase (i) was activated by FMN. | | | |
Reference
| Z. Naturforsch. 36c, 400 (1981); received February 23/M arch 16 1981 | | | |
Published
| 1981 | | | |
Keywords
| NADH Dehydrogenase, Purification, Localization, Inhibitors, Rhodopseudomonas capsulata | | | |
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| | | | | TEI-XML for
| default:Reihe_C/36/ZNC-1981-36c-0400.pdf | | | | Identifier
| ZNC-1981-36c-0400 | | | | Volume
| 36 | |
| 11 | Author
| Klaus Pfister, H. Artm, K. Lichtenthaler, G. Ünther Burger, Hans Musso, M.Anuel Zahn | Requires cookie* | | | Title
| The Inhibition of Photosynthetic Light Reactions by Halogenated Naphthoquinones | | | | Abstract
| Halogenated naphthoquinones act as inhibitors o f photosynthetic electron flow. I50 concentra tion for inhibition of methylviologen reduction were found to range between 2 x 10-5 m to 2 x 10-6 M. Comparing their effects on several partial reactions o f electron flow, the inhibition site o f the naphthoquinones was found to be at the reducing site o f PS II. Studies o f fluorescence transients in presence o f halogenated naphthoquinones give further evidence for a site action similar to that o f diuron and different to that of DBMIB. All naphthoquinones act as quenchers o f chlorophyll fluorescence with pure chlorophyll a, and with much higher efficiency in green algae and chloroplasts. It is concluded, that the halogenated naphthoquinones act similar to PS II-inhibitors like diuron, but do not share a common binding site at the PS II-complex. Implications of a possible involvement of phylloquinone K 1 in photosynthetic electron transport are discussed. The synthesis o f 2-chloro-as well as 2-bromo-3-isopropyl-1,4-naphthoquinone is described. | | | |
Reference
| Z. Naturforsch. 36c, 645—655 (1981); received April 271981 | | | |
Published
| 1981 | | | |
Keywords
| Chlorophyll Fluorescence, Electron Transport, Inhibitors, Naphthoquinones, Photosynthesis, Quenchers | | | |
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| | | | | TEI-XML for
| default:Reihe_C/36/ZNC-1981-36c-0645.pdf | | | | Identifier
| ZNC-1981-36c-0645 | | | | Volume
| 36 | |
| 12 | Author
| Jacek Wierzchowski, David Shugar | Requires cookie* | | | Title
| Sensitive Fluorimetric Assay for Adenosine Deaminase with Formycin as Substrate; and Substrate and Inhibitor Properties of some Pyrazolopyrimidine and Related Analogues | | | | Abstract
| The nucleoside antibiotic formycin, 7-amino-3-(/?-D-ribofuranosyl)pyrazolo(4,3-d)pyrimidine, a structural analogue of adenosine, is deaminated about 10-fold faster by adenosine deaminase than adenosine itself, and is therefore a superior substrate for both routine assays and kinetic studies with the purified enzyme. The luminescence properties o f formycin have been profited from to develop a fluorimetric assay for adenosine deaminase which is considerably more sensi tive than the spectrophotometric procedure widely employed with adenosine as substrate. Exam ples are presented of its application to routine assays of adenosine deaminase levels in cellular extracts, as well as to kinetic studies with the purified enzyme, including the properties o f some pyrazolopyrimidine and purine substrates and inhibitors. | | | |
Reference
| Z. Naturforsch. 38c, 67—7 (1983); received August 23 1982 | | | |
Published
| 1983 | | | |
Keywords
| Formycin, Pyrazolopyrimidines, Adenosine Deaminase, Fluorimetric Assay, Inhibitors | | | |
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| default:Reihe_C/38/ZNC-1983-38c-0067.pdf | | | | Identifier
| ZNC-1983-38c-0067 | | | | Volume
| 38 | |
| 13 | Author
| Friedrich Jiittner, O. Ttm Ar Bogenschütz | Requires cookie* | | | Title
| Geranyl Derivatives as Inhibitors o f the Carotenogenesis in Synechococcus PCC 6911 (Cyanobacteria) | | | | Abstract
| The ability of several geranyl derivatives to inhibit carotenoid synthesis in Synechococcus (Cyanobacteria) was measured using a cyanobacterial bioassay. The inhibitory activity o f differ ent molecules varied according to chain length and substituents. Pseudoionone, famesyl acetate, geranyl acetate, geranial and farnesol proved to be the most active derivatives tested. 6-Methylhept-5-en-2-one, farnesyl acetone, linalool and geranyl linalool exhibited no effect when employed in concentrations as high as 100 ppm. Besides phytofluene, C-carotene was accumu lated after application o f sublethal amounts o f active geranyl derivatives. Cell growth and chlorophyll a synthesis were only slightly affected under conditions were carotenoid synthesis was markedly inhibited. | | | |
Reference
| Z. Naturforsch. 38c, 387 (1983); received January 26 1983 | | | |
Published
| 1983 | | | |
Keywords
| Inhibitors, Carotenoid Synthesis, Pseudoionone, Famesol, Famesyl Acetate | | | |
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| | | | | TEI-XML for
| default:Reihe_C/38/ZNC-1983-38c-0387.pdf | | | | Identifier
| ZNC-1983-38c-0387 | | | | Volume
| 38 | |
| 15 | Author
| | Requires cookie* | | | Title
| Phosphorylation of Coformycin and 2 -Deoxycoformycin, and Substrate and Inhibitor Properties of the Nucleosides and Nucleotides in Several Enzyme Systems | | | | Abstract
| Under conditions where 2'-deoxycoformycin is enzymatically phosphorylated by wheat shoot phosphotransferase to the 5'-phosphate in 15—20% yield, coformycin is a relatively poor sub strate, and is phosphorylated only to the extent of < 5%. However, chemical phosphorylation of coformycin by modifications of the Yoshikawa procedure led to isolation of coformycin-5'-phos phate in 20% overall yield. Coformycin-5'-phosphate was characterized by various criteria, including 'H NMR spectro scopy. Comparison of the spectrum with that of the parent nucleoside indicated that the nu cleotide is predominantly, although not exclusively, in the conformation anti about the glycosidic bond. Like 2'-deoxycoformycin-5'-phosphate, coformycin-5'-phosphate was a feeble substrate of snake venom 5'-nucleotidase, and is hydrolyzed, quantitatively, at only 2% the rate for 5'-AMP. With 5'-AMP analogues as substrate, the 5'-phosphates of both coformycin and deoxycoformycin were poor inhibitors of the enzyme, with K, values > 0.3 mM. The 5'-phosphates of both coformycin and deoxycoformycin do not significantly inhibit adenosine deaminase (K} > 0.2 m M), but are potent inhibitors of adenylate deaminase (Kj < 10"9 m). Neither coformycin nor deoxycoformycin are inhibitors of mammalian purine nucleoside phosphorylase. The stabilities of coformycin, deoxycoformycin, and their 5'-phosphates, have been examined as a function of pH, and nature of the buffer medium. In particular, all exhibit instability in acid and neutral media, but are relatively stable in the vicinity of pH 9. Some biological aspects of the overall results are presented. | | | |
Reference
| Z. Naturforsch. 40c, 710—714 (1985); received March 5/June 3 1985 | | | |
Published
| 1985 | | | |
Keywords
| Coformycin, 2'-Deoxycoformycin, Phosphorylation, 5'-Phosphates, Substrates, Inhibitors | | | |
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| | | | | TEI-XML for
| default:Reihe_C/40/ZNC-1985-40c-0710.pdf | | | | Identifier
| ZNC-1985-40c-0710 | | | | Volume
| 40 | |
| 16 | Author
| MitkoA. Subchev, JuliusA. Ganev, Otto Vostrowsky, HansJürgen Bestmann | Requires cookie* | | | Title
| Screening and Use of Sex Attractants in Monitoring of Geometrid Moths in Bulgaria | | | | Abstract
| Four candidate sex attractants for geometrid moths have been screened individually and in mixtures. As a result, in addition to the confirmation of the known sex attractants of Operophtera brumata L. and Alsophila aceraria Denis & Schiff (— A. quadripunctata Esper), possible sex attractants for five other geometrid species have also been established. For O. brumata and A. aceraria an inhibitor has been found. For the same species the possibility for seasonal monitoring by means of sex pheromone traps was demonstrated. | | | |
Reference
| Z. Naturforsch. 41c, 1082—1086 (1986); received May 7 1986 | | | |
Published
| 1986 | | | |
Keywords
| Pheromones, Sex Attractants, Geometridae, Polyene Hydrocarbons, Inhibitor | | | |
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| | | | | TEI-XML for
| default:Reihe_C/41/ZNC-1986-41c-1082.pdf | | | | Identifier
| ZNC-1986-41c-1082 | | | | Volume
| 41 | |
| 17 | Author
| Rekha Chaturvedi, M. Singh, P. V. Sane | Requires cookie* | | | Title
| Photoinactivation of Photosynthetic Electron Transport under Anaerobic and Aerobic Conditions in Isolated Thylakoids of Spinach | | | | Abstract
| The effect o f exposure to strong white light on photosynthetic electron transport reactions o f PS I and PS II were investigated in spinach thylakoids in the absence or presence o f oxygen. Irrespective o f the conditions used for photoinactivation, the damage to PS II was always much more than to PS I. Photoinactivation was severe under anaerobic conditions compared to that in air for the same duration. This shows that the presence o f oxygen is required for prevention o f photoinactivation o f thylakoids. The susceptibility o f water-splitting com plex in photoinactivation is indicated by our data from experiments with chloride-deficient chloro-plast membranes wherein it was observed that the whole chain electron transport from DPC to MV was much less photoinhibited than that from water. The data from the photoinactivation experiments with the Tris-treated thylakoids indicate another photodam age site at or near reaction centre o f PS II. D CM U -protected PS II and oxygen-evolving com plex from p h oto inactivation. D C M U protection can also be interpreted in terms o f the stability o f the PS II complex when it is in S2 state. | | | |
Reference
| Z. Naturforsch. 47c, 63—6 (1992); received August 16 1991 | | | |
Published
| 1992 | | | |
Keywords
| Photoinactivation, Anaerobiosis, Inhibitors, Photosynthetic Electron Transport, Trypsinization | | | |
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| default:Reihe_C/47/ZNC-1992-47c-0063.pdf | | | | Identifier
| ZNC-1992-47c-0063 | | | | Volume
| 47 | |
| 18 | Author
| M. O. Ilori, O. O. Amund, O. Omidiji | Requires cookie* | | | Title
| Characterisation of a Neutral Protease Produced by Micrococcus luteus | | | | Abstract
| A proteolytic enzyme produced by a cassava-ferment ing strain of Micrococcus luteus was extracted and puri fied 50-fold by gel filtration and ion exchange chroma tography. The optimum pH for the enzyme was 7.0, the opti mum temperature 25 °C, the apparent molecular weight 42 kDa and the K m value, 0.45 mg m l-1 with casein as substrate. The enzyme was stimulated by Ca2+ and Mg2+ but inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, KCN, citric acid and L-cysteine indicating the enzyme to be a metalloprotease. | | | |
Reference
| Z. Naturforsch. 51c, 429—431 (1996); received May 26 1995/January 15 1996 | | | |
Published
| 1996 | | | |
Keywords
| M etalloprotease Purification, Heat Inactivation, Apparent Molecular Weight, Inhibitors | | | |
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| default:Reihe_C/51/ZNC-1996-51c-0429_n.pdf | | | | Identifier
| ZNC-1996-51c-0429_n | | | | Volume
| 51 | |
| 19 | Author
| M.-L Heskamp, W. Barz | Requires cookie* | | | Title
| Characterization of Proteases from Rhizopus Species after Growth on Soybean Protein | | | | Abstract
| Culture filtrates of different fungi of the genus R hizopus forming tem pe (i.e. traditional Indonesian food) were grown on a soybean protein-raffinose-phytate medium and investi gated for protease activity using soyprotein as substrate. A ll isolates belonging to the species R. oryzae, R. stolonifer, R. oligosporus, and R. m icrosporus var. chinensis, formed the well-known R hizopus-pepsin (aspartic proteinase, 35 kD, isoelectric points: 5.9, 5.0, <4) and an additional protease mainly active under alkaline conditions. The new protease (33 kD, iso electric points: variable and isolate specific) was purified approximately 300-fold and shown to be a serine protease (inhibitor studies). During fungal culture (1 2 -1 3 5 h) the aspartic proteinase is expressed first followed by the serine protease. Both proteases are insensitive to the soybean Kunitz and Bowman-Birk inhibitors. The best rate of soyprotein degradation is achieved by the coordinate action of both proteases at pH 6.5. The examined R hizopus isolates differ in the time course and intensity o f the expression o f the alkaline protease. | | | |
Reference
| Z. Naturforsch. 52c, 595 (1997); received May 6/July 3 1997 | | | |
Published
| 1997 | | | |
Keywords
| Soyprotein, R hizopus, Proteases, Tempe, Inhibitors | | | |
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| | | | | TEI-XML for
| default:Reihe_C/52/ZNC-1997-52c-0595.pdf | | | | Identifier
| ZNC-1997-52c-0595 | | | | Volume
| 52 | |
|
