Two clones that contain goat growth hormone (gGH) genes were isolated from goat genomic library using goat growth hormone cDNA as a probe. One clone CgGH contained gGHl gene, and another clone, EgGH, contained gGH2 and gGH3 genes. The clone EgGH contained 491 bp inserted sequence, just upstream of the gGH3 gene, which was not present in the clone CgGH. From the sequencing data of the flanking regions of these gGH genes, short interspersed repetitive sequences (SINES) were found. Four SINES's existed in the CgGH clone and eight SINES's existed in the EgGH clone. The number of the repetitive DNA sequences in the goat genome was estimated about 10² copies from the analysis of the reassociation rate. As the number of gGH genes (gGHl, gGH2, and gGH3) per genome was different among individual goats, DNA fragments containing gGHl gene, and that containing gGH2 and gGH3 genes, were estimated to be allelic on the goat chromosome.

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By immunoblotting using monoclonal and polyclonal mouse antibodies against sweet potato (Ipomoea batatas (L.) Lam.) starch phosphorylase (SP), and by activity and dye staining methods, fresh extracts obtained from sweet potatoes immediately after harvest or from those being stored under various conditions were analyzed for SP by PAGE. Freshly prepared pure or crude SP, or those stored under various conditions were also analyzed. We found that the native enzyme from either of the cultivars Tainong 57 or 65 was 220-kDa in size and constituted of two 112-kDa subunits. Either in vivo or in vitro, storage caused degration of the enzyme to two groups of small subunits of about 50-kDa each. On prolonged cold storage of purified enzyme in 50% glycerol, the formation of a small amount of a 250-kDa protein was detected. It had a 150-kDa subunit that was formed presumably by transpeptidation catalyzed by a contaminating protease. This 250-kDa form had the primed SP activity only. The SP from the two kinds of cultivar showed considerable differences in the proteolytic susceptibility and peptide map. A part of Tainong 65 SP was supposed to be a heterodimer.

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We report here the difference between phenyl propanoid glycosides obtained from hot water and methanol extracts of lemon peel. Eight phenyl propanoid glycosides were isolated, and their structures were established by UV, MS, ¹H-NMR and ¹³C-NMR spectroscopy, as well as by chemical evidence. They were coniferin (1), syringin (2), dehydrodiconiferyl alcohol-4-β-glucoside (3), citrusin A (4), citrusin B (5), citrusin C (6), methyl-3-(4-β-glucopyranosyl-3-methoxyphenyl)propionate (7) and methyl-3-{4-(6-O-α-glucopyranosyl-β-glucopyranosyl)-3-hydroxyphenyl}propionate(8). Compound 7, after intravenously injecting (0.5 mg/100 g of body weight) into stroke-prone spontaneously hypotensive rats (SHR-SP), was found to lower the blood pressure. Among these isolated compounds, 7 and 8 are new phenyl propanoid glycosides.

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Phosphatase activity, using p-nitrophenyl phosphate (NPP) as the substrate, was inhibited by myo-inositol hexaphosphate (phytate). The extent of inhibition by 5 mM phytate of the alkaline phosphatase activity of calf intestine and Escherichia coli, and of the acid phosphatase activity of wheat germ was 82, 56 and 50%, respectively. However, acid phosphatases from rice bran were not inhibited by 10 mM phytate. The effect of preincubation with phytate on the acid and alkaline phosphatase activity was investigated. After a 180-min preincubation with 1 mM phytate, the extent of inhibition was 98% for the calf intestine enzyme, 88% for the E. coli enzyme, and 75% for the wheat germ enzyme. Mg²⁺ enhanced the phosphatase activity, but the addition of phytate lowered it. The inhibition of E. coli alkaline phosphatase by phytate was noncompetitive, with an apparent inhibitor constant of 0.45 mM under the assay conditions. The inhibition of calf intestine alkaline phosphatase and of wheat germ acid phosphatase was of the mixed type, with inhibitor constants of 0.13 mM and 0.43 μM, respectively. Therefore, phytate may interact with a complex of these phosphatases and substrates.

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Milk caseins were modified by glucose at 50°C and RH75% for 1 day (CG-1), 7 days (CG-7) and 14 days (CG-14), and at 95°C in an aqueous solution (CG-95). The nutritional and physiological effects of these browned caseins supplemented with lost amino acid were investigated on growing and adult rats.
Biochemical values for hematocrit, erythrocyte, leucocyte, GOT, GPT, triglyceride and cholesterol in serum were unchanged between the experimental and the control group. However, serum glucose of the browned casein-fed group was significantly decreased. The weight gain of rats fed with browned casein was inhibited, the extent of inhibition depending on the degree of modication of the casein by glucose. CG-7 had an inhibitive effect on the weight gain of both growing and adult rats. There was no difference in the nutritional and physiological effects between CG-7 and CG-95 casein. In addition, the weight gain of rats fed with the nondialyzed browned casein-glucose reaction mixture was significantly lower than of those fed with the dialyzed browned casein-glucose reaction mixture. From these results, it was estimated that some antinutritional substances were produced during the Maillard reaction of casein with glucose under various conditions.

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NAD(P)-Dependent L-sorbosone dehydrogenase has been purified from the cytosol fraction of Gluconobacter melanogenus UV10. The enzyme was purified about 30-fold with an overall yield of 19% by column chromatographies on DEAE-Sepharose CL-6B, DEAE-Sephadex A-50, and Blue Sepharose CL-6B. The enzyme required NAD or NADP as a cofactor, and showed broad substrate specificity on various aldehyde compounds. Among them, L-sorbosone was the best substrate for the enzyme. In this respect, the enzyme is a kind of aldehyde dehydrogenase.

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The synthesis of Xylosyloligosaccharides from β-(1 → 4)-xylobiose in the presence of D-mannose by transxylosylation with β-xylosidase from Aspergillus niger IFO 6662 was studied. At first, the transxylosylation products were separated by charcoal column chromatography in 5% ethanol elution into three peaks, P-l, P-2, and P-3. They were further separated on thin layer chromatography, and their three products, saccharides O-4, O-5, and O-N were purified by preparative paper chromatography. Saccharides O-4 and O-5 were identified as O-β-D-xylopyranosyl-(1 → 4)-D-mannopyranose and O-β-D-xylopyranosyl-(1 → 6)-D-mannopyranose, respectively, by measurement of the degree of polymerization, specific rotation, acid hydrolysis, and methylation analysis. By ¹H-NMR spectroscopy in addition to these analyses, saccharide O-N was identified as O-β-D-xylopyranosyl-(1 → 1')-β-D-xylopyranose, a new nonreducing xylobiose.

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A mutant unable to grow under acidic conditions was isolated from the acidophilic heterotrophic bacterium Acidiphilium fadlis 24R. The growth of the mutant could be fully restored by the addition of spermidine or lysine at the concentration of 100 μM. The HPLC analysis of polyamine composition showed that spermidine and putrescine were major polyamine components in the parental strain. In the mutant strain, putrescine was replaced by cadaverine. It was found that some polyamines in the cells were conjugated with the other cell components. The growth of the bacterium in the medium below pH 4.5 was inhibited in the presence of α-methylornithine or methylglyoxal-bis(guanylhydrazone), which are inhibitors of rate-limiting enzymes involved in the biosynthesis of polyamines. The growth of the bacterium that had been inhibited in the presence of inhibitors could be fully restored by the addition of putrescine or spermidine. On the basis of these results, it was concluded that polyamines have a significant role in the growth of Aicidiphilium fadlis 24R under acidic conditions.

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A maltotriose-producing amylase, which hydrolyzes the α-l, 4-glucosidic linkages in starch with maltotriose units was found in the culture filtrate of a strain of the genus Microbacterium newly isolated from soil. The enzyme was purified almost to homogeneity by ammonium sulfate fractionation, DEAE-Sepharose column chromatography and Sephadex G-150 column chromatography. Its optimum pH and temperature were around 6.5-7.0 and around 50°C, respectively. The enzyme was protected from heat in the presence of calcium ion. Its molecular weight was estimated to be about 40, 000 by the gel filtration method. Typical sugar composition of hydrolysis products from liquefied starch was about 55-60% of maltotriose, 10-20% of maltose, 1-3% of glucose and 20-40% of other higher oligosaccharides.

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At least fourteen or fifteen kinds of endo-xylanase components (endo-X) were found to participate in the xylan-hydrolysing activity of the mid-gut gland of the apple snail (Pomacea canaliculatd). One of these endo-X was purified to electrophoretic homogeneity from the mid-gut glands of the female snails. Its molecular weight and isoelectric point were estimated to be about 42, 000 by SDS-PAGE and 7.45, respectively. The optimum pH of the enzyme reaction existed between 6.0-6.3, and the activity was stable from pH 4.5-9.0, and was stable for 15min at 40°C and pH 6.0. The activity of this enzyme rose markedly in the presence of some chlorides or sodium bromide, but not in the presence of sodium sulfate or sodium citrate.

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Indole-3-acetic acid (IAA) was identified as a tryptophan (Trp) catabolite in the cultures of Enterobacter cloacae isolated from the rhizosphere of well-grown cucumbers. This strain produced IAA in a tryptophan-supplemented liquid medium at levels of up to 1 mg/ml, and indole-3-lactic acid (ILA) and tryptophol (Tol) were also produced. Under aerobic conditions, IAA was produced in higher concentrations than ILA and Tol, but under less aerobic conditions, ILA and Tol were produced in higher concentrations than IAA. In metabolic studies with eight kinds of indole substrates, E. cloacae converted Trp, indole-3-pyruvic acid (IPyA), and indole-3-acetaldehyde (IAAld) to IAA. These results strongly suggest that the biosynthesis of IAA in E. cloacae involves the pathway of Trp to IAA via IPyA and IAAld.

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A proteinase inhibitor was purified from the seeds of faba bean (Vicia faba L.) to an electrophoretically homogeneous protein by extraction, salting-out, and column chromatographies on CM-Sephadex C-25, Sephadex G-75, and QAE-Sephadex A-25. The inhibitor (FBPI) was a basic protein with a molecular weight of 7000 and an isoelectric point of 8.7. The amino acid composition had a fairly high content of half-cystine and lacked of methionine, isoleucine, and tryptophan. FBPI inhibited bovine trypsin and α-chymotrypsin in a 1:1 (M/M) stoichiometry: the Ki's were 6.1×10^-9 M and 4.4 × 10^-8 M, respectively. The inhibitor was stable in acidic and neutral pH, but it lost its activity upon heat treatment at alkaline pH. These properties indicate that FBPI belongs to the Bowman-Birk soybean proteinase inhibitor family.

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An antimicrobial substance produced by Pseudomonas cepacia B5 (B5) against the bacterial wilt disease pathogen, Pseudomonas solanacearum, was isolated and identified in order to clarify the mechanism for disease suppression by B5. A filtrate of the B5 culture showed high inhibitory activity against this pathogen. The active substance was isolated in pure form by chromatography with a Diaion HP20 column and by high-performance liquid chromatography with a Jaigel GS220 column. On the basis of IR, NMR, and mass spectra, the antimicrobial substance was identified as 2-keto-D-gluconic acid (2KGA). The production of 2KGA and the destruction of the disease pathogen in a contaminated soil suspension to which the B5 strain was added, together with wheat bran, suggested that 2KGA might be involved in disease suppression by P. cepacia B5.

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We examined the products from the reaction of N^α-acetyltryptophan (Ac-Trp) and hexanal, which is a major secondary product of lipid peroxidation, in the presence of cations such as N^α-acetyllysine. N^α-Acetyl-1-(1-hydroxyhexyl)tryptophan (Trp-HL-4) was identified as a major product in addition to cross-linking products of Ac-Trp which we had reported in a previous paper [Kaneko et al., Agric. Biol. Chem., 53, 2679 (1989)]. Trp-HL-4 was assumed to be an intermediate through a cross-link formation. The course of browning of Ac-Trp derivatives was also examined and their role in browning and fluorescence production in proteins was discussed.

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Prior to investigating the freeze drying of liquid foods, the freeze drying of a water-glass bead system was analyzed by a conventional uniformly retreating ice front (URIF) model. The drying rate gradually changed as drying proceeded (phase I) until a certain critical time, and then sharply decreased (phase II), probably due to instability in the sublimation plane. The apparent thermal conductivity of the frozen layer estimated by using the drying data from phase I agreed well with the thermal conductivity calculated by the Kunii-Smith model. This result shows that the heat flow through the dry layer, to which both heat conduction and heat transfer accompanied by vapor flow would contribute, was small enough compared with that from a heater in the present drying system. The drying rate and the temperature of the frozen layer in phase I were described well by the conventional URIF model.

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The freeze drying of liquid foods was analyzed by a modified uniformly retreating ice front (URIF) model, where the unfrozen water and the surface resistance of the material were considered. The apparent thermal conductivity estimated by the data for drying was approximately twice as large as the thermal conductivity measured by the steady state method. The vapor permeability and surface resistance was separately estimated from the apparent thermal conductivity, the volume fraction of ice crystals in the sample, and from the drying data. The vapor permeability was higher as the initial water content was higher and the freezing temperature was higher. The surface resistance was higher as the initial water content was lower and the freezing temperature was lower. The drying rate and the temperature of the frozen layer were well described by the modified URIF model with the apparent thermal conductivity, the vapor permeability and the surface resistance.

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Streptococcal antitumor protein (SAGP) was produced by transformed E. coli JM103 carrying the SAGP gene downstream from the tac promoter. The purified recombinant SAGP had the same N-terminal amino acid sequence as that of the native SAGP isolated from Streptococcus pyogenes Su cells. Gel filtration analysis showed that the recombinant SAGP was a dimer, while the native SAGP was a tetramer. When the antitumor activity was tested against sarcoma 180 cells, the IC₅₀ of the recombinant SAGP was 0.3 μ/ml, about a quarter as active as the native SAGP. These results suggest that the quaternary structure of SAGP is important for the antitumor activity.

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The surface lipids of Nicotiana umbratica contained several varieties of glycolipids. Three types of glucose esters and five types of sucrose esters were isolated and identified from this species. These glycolipids contained short-chain fatty acids such as acetic, methylpropionic, methylbutyric, 3-methylpentanoic, 4-methylpentanoic and methylhexanoic acids. The acetylated positions of each compound were determined by 2-D NMR, using the HMBC technique. The structures of the glucose esters were l, 6-di-

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Aromatic acid reductase (aryl-aldehyde dehydrogenase, EC 1.2.1.30) was purified to electrophoretic homogeneity from Nocardia asteroides JCM 3016. The enzyme was a monomeric protein with a molecular weight of 152, 000. The enzyme absolutely required ATP, NADPH, and MgCl₂ for the reduction of benzoate to benzaldehyde. In the overall reaction, benzaldehyde, AMP, and NADP⁺ were stoichiometrically formed from benzoate, ATP and NADPH, respectively. The purified enzyme catalyzed the reduction of benzoyl adenosine 5'-monophosphate (bzAMP), which is the intermediate formed from benzoate and ATP. The temperature dependence of the benzoate- and bzAMP-reducing activities agreed exactly, and the same Km for NADPH was obtained by the steady state kinetics of both reactions. These results suggest that the overall reduction of benzoate proceeds via bzAMP, and that the ATP-dependent adenylation of benzoate and the reduction of bzAMP are catalyzed by one enzyme. The enzyme was fairly specific for meta-substituted benzoates.

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Photolysis of the fungicide flutolanil, 3'-sopropoxy-2-(trifluoromethyl)benzanilide, was investigated both in an aqueous solution and on solid surfaces (silica gel and glass) by irradiating with UV light under laboratory conditions. In an ethanolic aqueous solution, irradiation resulted in the formation of a major product [2-(trifluoromethyl)benzamide] and some other products [2-(trifluoromethyl)benzoic acid, N-ethoxycarbonyl-2-(trifluoromethyl)benzamide, etc.]. The latter is considered to have been formed by the reaction with an organic solvent. On the solid surfaces, the main photoproduct was 2'-amino-4'-isopropoxyphenyl 2-(trifluoromethyl)phenyl ketone, a product from the photo-Fries rearrangement reaction. Another photoproduct, 3'-hydroxy-2-(trifluoromethyl)benzanilide was obtained only on the glass surface, this desisopropylated compound not being detected under any other conditions. The photolysis of this fungicide, was accelerated more by carbonyl compounds such as benzophenone, acetophenone, flavone and xanthone than by dye photosensitizers like rose bengal, chlorophyllin and riboflavin.

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Activities of seven enzymes of the shikimate pathway were compared between the wild-type strain and menaquinone-4-producing mutant strains of Flavobacterium sp. 238-7. Activity of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthase, the first regulatory enzyme in the shikimate pathway, was almost the same in these strains in the stationary phase, but the activity of a sulfonamide-resistant strain, SP0736, was 2 times higher than that of other strains in the logarithmic phase. Shikimate dehydrogenase activity was almost the same among these strains during cultivation. Other enzyme activities of mutants were 1.5-4 fold higher than those of the wild-type strain. DAHP synthase and shikimate kinase were found to be inhibited by chorismate and MK-4. Feedback inhibition for shikimate kinase by chorismate was partially removed in strain SP0736.

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The mode of action of the nuclease from the fruit body of Flammulina velutipes was studied. The nuclease hydrolyzed single-stranded linear polynucleotides exonucleolytically from the 5'-end to produce 5'-mononucleotides. The nuclease also cleaved a single strand of circular DNA endonucleolytically. Single-stranded circular DNA was cleaved by the nuclease to single-stranded linear DNA. The nuclease converted double-stranded circular DNA, which is covalently closed circular DNA, to linear DNA via open circular DNA. Thus the nuclease has both exo- and endonucleolytic activities.

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Temperature-induced changes in lipid molecular species of a thermophilic cyanobacterium, Mastigocladus laminosus, were investigated. The cells were grown at 48°C phototrophically, and transferred at mid-log phase to 40°C and 55°C. The lipids in the cells grown at different temperatures were extracted, analyzed, and compared. The cells acclimated to decreasing and increasing temperatures by altering the constituent longer fatty acids and lipid class levels. The variation in fatty acids caused great changes in molecular species of lipids. The ways of changing lipid molecular species may have differed among lipid classes. Thermal analysis of the lipids showed that thermograms of the membrane lipids were greatly affected by the growth temperature, suggesting that proper changes in the membrane fluidity are required.

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Three bacterial strains, A41, B47, and MM4, isolated from sea sediment and aeration tanks of a sewage plant, identified as Pseudomonas stutzeri, showed lethal activity against the red tide phytoplankton Chattonella antiqua. Upon the addition of the culture broth of bacteria, C. antiqua lost its mobility and lysed. Their lethal activity reached a maximum in the nutrient broth containing 3% NaCl at 25°C (the lowest lethal concentration; 0.5%) for 2 to 6 days of cultivation. Addition of the A41 culture broth to a coculture of C. antiqua and killifish (Oryzias latipes) showed the selective toxicity on C. antiqua.

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Two types of fucan sulfates, galactofucan sulfate and fucoidan, which were isolated separately from the fronds of the brown seaweed Ecklonia kurome, were fractionated according to molecular weight by gel filtration on a Sepharose CL-6B column. The five galactofucan sulfate subfractions (molecular weights; 10, 000 to 79, 000) and three fucoidan subfractions (13, 000 to 58, 000) obtained were composed of fucose, galactose, xylose, glucuronic acid, and sulfate in the approximate molar ratios of 1.00:0.49-0.93: nil-0.08:0.02-0.05:1.56-1.76 and 1.00:0.10-0.21: nil: 0.02-0.05: 1.42-1.56, respectively. The relationship between the molecular weight and the anticoagulant activity of the two types of fucan sulfates was studied. Both of the fucan sulfates with molecular weights ranging from about 10, 000 to 300, 000 showed the most potent specific activities in the activated partial thromboplastin time (APTT) assay. In contrast, antithrombin activity of both fucan sulfates was found to be dependent on their molecular weight up to a molecular weight of about 50, 000.

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Dietary fibers, alginate and defatted corn fiber, adsorbed food mutagens, Trp-P-1 and Glu-P-1, which are heterocyclic amines formed in cooking processes. The saturation masses of adsorbed heterocyclic amines to unit mass of the alginate, and to the defatted corn fiber, in distilled water, were independent of the specific surface area of the dry fibers. The saturation mass of Trp-P-1 to the alginate was more than twenty times as much as that to the defatted corn fiber, binding of 0.8 mol, or more, of Trp-P-1 per 1 mol of uronic acid of alginate. Pectic acid, another polymer of uronic acid, also had high binding capacity for Trp-P-1 and Glu-P-1, but chitosan, a polymer of glucosamine, adsorbed neither Trp-P-1 nor Glu-P-1. Dimethylnitrosoamine, which is also a food mutagen, was not adsorbed to these dietary fibers. These results suggested that the heterocyclic amines were mostly adsorbed to the carboxyl groups of the dietary fibers.

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Oryzalides A and B, and oryzalic acid A, which were isolated from healthy flag leaves of a bacterial leaf blight-resistant cultivar of rice plant as a group of novel antimicrobial compounds, were confirmed by chemical and spectroscopic studies to be ent-kaurane (C₁₉ and C₂₀) or ent-kaurene (C₁₉) analogues, i.e., oryzalide A, ent-15α, 16-epoxy-1β-hrydroxy-2-oxa-kauran-3-one; B, ent-1β, 15αdihydroxy-2-oxa-16-kauren-3-one; and oryzalic acid A, ent-15α, 16-epoxy-2, 3-secokauran-2, 3-dioic acid.

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The effects of whey protein and casein (both as a 25% diet) on plasma and liver lipids were compared in male Wistar rats. The plasma cholesterol level was significantly decreased in rats fed with a whey protein diet, compared with casein supplemented with or without cholesterol. These changes in plasma cholesterol were observed continuously for 70 days throughout the experiment. The concentrations of total lipids, cholesterol and phospholipid in liver were significantly decreased in rats fed with a whey protein diet compared to casein supplemented with cholesterol. There was a significantly higher influx of lipoprotein cholesterol into the plasma compartment after a casein diet than after a whey protein diet containing high cholesterol. These data suggest that dietary protein may induce different plasma lipids levels by modulating the rate of lipid influx into the plasma compartment in rats fed with a cholesterol-supplemented diet.

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Assays for typical pyrethroidal insecticides were developed to determine their absolute purity. Resmethrin, furamethrin and phenothrin could be determined by a neutralizing titration after hydrolyzing with potassium hydroxide to achieve relative standard deviations (RSD) of 0.10, 0.19 and 0.35%, respectively. Allethrin, phthalthrin and furamethrin could be determined by a neutralizing titration in a non-aqueous solvent after reacting with ethylenediamine to achieve RSD values of 0.10, 0.14 and 0.09%, and permethrin by a chlorine determination with the oxygen combustion method to achieve RSD of 0.23%. These methods are effective for assays of the reference standards because there is no necessity for another reference standard.

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It has been suggested that peptide inhibitors of prolyl endopeptidase (PEP) may act as anti-amnestic agents. In the hope of finding PEP inhibitors in milk proteins, we synthesized a total of 37 human β-casein peptide fragments containing proline residues. It was found that the peptides with PEP inhibition activity in vitro were located in the region of amino acid residues 49-59 of human β-casein. The most potent inhibitor was Ile-Tyr-Pro-Phe-Val-Glu-Pro-Ile (IC₅₀ = 8μM).

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We screened for foodstuffs affecting interferon-β (IFN-β) production of human foreskin diploid fibroblasts, in the presence of poly I poly C, cycloheximide, and actinomycin D. α- and β-caseins stimulated IFN-β production dose-dependently, but κ-casein inhibited it. Of the two chymosin fragments of κ-casein, glycomacropeptide was an inhibitor but p-κ-casein was not. β-lactoglobulin stimulated IFN-β production weakly, but lactoferrin inhibited it strongly. It was also shown that serum contained some factors inhibiting IFN-β induction and stimulating its production.

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The inhibitory effects of 3-nitro-2, 4, 6-trihydroxybenzamide derivatives on human 5-lipoxygenase (5-LO), a key enzyme in arachidonic acid cascades, were examined using 5-LO produced by Escherichia coli. Some of the tested compounds inhibited the conversion of arachidonic acid to 5-hydroperoxy-6, 8, ll, 14-eicosatetraenoic acid (5-HPETE), and in particular the N-phenylbutyl derivative was about 30 times more active (IC₅₀ = 35μM) than caffeic acid (IC₅₀ = 1000 μM), a known selective 5-LO inhibitor.

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Ethylene glycols and polyethylene glycols inhibited the growth of a photosynthetic bacterium, Rhodopseudomonas acidophila, strain M402 under aerobic-dark and anaerobic-light culture conditions. However, polyethylene glycol dehydrogenating activity was demonstrated with phenazine methosulfate (PMS) as an electron acceptor in parallel with the PMS-linked aromatic alcohol dehydrogenase activity. Addition of ethylene glycols or polyethylene glycols to the culture neither induced aromatic alcohol dehydrogenase, nor accelerated polyethylene glycol dehydrogenating activity. Purified PMS-linked aromatic alcohol dehydrogenase had high affinities toward diethylene glycol and polyethylene glycols. This indicated that the dye-linked aromatic alcohol dehydrogenase is capable of oxidizing these xenobiotic synthetic polymer alcohols, polyethylene glycols. There is no evidence on the existence of a specific polyethylene glycol dehydrogenase in this bacterium.

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