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PubMed1995

Effect of cellular type on expression of acid beta-glucosidase: implications for gene therapy in Gaucher disease.

The effects of cellular type on the expressed activity of acid beta-glucosidase were evaluated using retroviral constructs containing the human cDNA. MFG retroviral ecotropic and amphotropic vectors containing the human acid beta-glucosidase cDNA were produced and used to infect different murine cell lines (fibroblast, neuronal and monocytic) and human cells (HL60 and cord blood CD34+), respectively. The expression of human acid beta-glucosidase was evaluated by enzyme activity assays, quantitative Western blots and immunofluorescence. All cells permanently integrated viruses and expression of enzyme protein was achieved in all cell lines, but cellular transduction efficiency differed even between different neuronal cell lines (eg N18S > PC12). In most cell lines acid beta-glucosidase activity was increased between two- and three-fold with concomitant signal increases by Western blot and immunofluorescence N18S cells had poor transduction efficiency, but high cellular expression in transduced cells. In NIH3T3 and MC3T3-E1 cells acid beta-glucosidase protein was expressed in 2-, 7- and 14-day cultures after infection and at least to passage four. The expressed acid beta-glucosidase in NIH3T3 cells was at two to three times normal activity levels, and was processed similarly to the human fibroblast enzyme. Inactive human acid beta-glucosidase was expressed in MC3T3-E1 preosteoblastic cells and this was maintained during differentiation to osteoblasts. These results indicate that gene transfer results in cell lines may not be generally extrapolated to all cells in tissues or to differentiated progeny.

3T3 Cells↗

PubMed1984

Biochemical genetics of the Lapland dog model of glycogen storage disease type II (acid alpha-glucosidase deficiency).

A recently described canine model (Lapland dog) of glycogen storage disease type II (GSD II, Pompe disease, acid alpha-glucosidase deficiency) was identified with several biochemical genetic methods. Complementation studies in which fibroblasts from a GSD II dog were fused with fibroblasts derived from control dogs and from human patients with different clinical forms of the disease did not lead to restoration of acid alpha-glucosidase activity in the heterokaryon cell populations. These results indicate that acid alpha-glucosidase deficiency is the primary defect in canine GSD II and that there is a close genetic parallelism with human GSD II. Immunotitration analysis of the residual acid alpha-glucosidase activity in the canine GSD II fibroblasts and liver demonstrated that this residual activity was not due to acid alpha-glucosidase enzyme, in which respect canine GSD II was similar to the infantile form of the human disease. Double immunodiffusion studies showed the presence of catalytically inactive acid alpha-glucosidase enzyme protein in canine GSD II. This is consistent with a structural gene mutation. It is concluded that canine GSD II in the Lapland dog is a homologous model of the infantile form of human GSD II, a conclusion in concordance with clinical and pathological studies.

Animals↗

PubMed1988

Active site directed inhibition of a cytosolic beta-glucosidase from calf liver by bromoconduritol B epoxide and bromoconduritol F.

Hydrolysis of p-nitrophenyl-beta-D-glucoside by cytosolic beta-glucosidase proceeds with retention of the anomeric configuration. Whereas inactivation of the enzyme by the glucosidase inhibitor conduritol B epoxide (CBE) was extremely slow (ki(max)/Ki 0.57 M-1 min-1) it reacted 130 times more rapidly with 6-bromo-6-deoxy-CBE (Br-CBE). The beta-glucosidase could be labeled with [3H]Br-CBE; incorporation of 1 mol inhibitor/mol enzyme resulted in complete loss of activity. Most of the bound inhibitor was released after denaturation and treatment with ammonia as (1,3,4/2,5,6)-6-bromocyclohexanepentol, thus demonstrating the formation of an ester bond with an active site carboxylate by trans-diaxial opening of the epoxide ring. It was concluded from the Ki values for the epoxide inhibitors and for coduritol B with the cytosolic enzyme and corresponding data for the lysosomal beta-glucosidase that the unusually low reactivity with CBE and Br-CBE is probably due to the inability of the cytosolic enzyme to effectively donate a proton to the epoxide oxygen. An extremely rapid inactivation of the cytosolic beta-glucosidase was caused by bromoconduritol F ((1,2,4/3)-1-bromo-2,3,4-trihydroxycyclohex-5-ene) with ki(max)/Ki 10(5) M-1 min-1. In contrast with the Br-CBE-inhibited enzyme the beta-glucosidase inhibited by bromoconduritol F was subject to spontaneous reactivation with t1/2 approximately 20 min.

Animals↗

PubMed1978

alpha-Glucosidase, a membrane-bound enzyme of alpha-glucan metabolism in Bacillus amyloliquefaciens. Purification and partial characterization.

The organism Bacillus amyloliquefaciens is capable of producing alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) and isoamylase (glycogen 6-glucanohydrolase, EC 3.2.1.68) extracellurlarly and a membrane-bound, intracellular alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20). The amounts of alpha-glucosidase in cells of B. amyloliquefaciens grown on amylaceous polysaccharides were significantly higher then in cells grown on non-carbohydrate carbon sources. alpha-Glucosidase was exclusively found associated with membranes from ruptured spheroplasts by subcellular fractionation and solubilization studies. Salt solutions and chelating agents alone did not dislodge alpha-glucosidase from membranes, but in combination with detergents were most effective in solubilizing active enzyme (0.1% sodium cholate (pH 8.0)/0.4 M sodium chloride). Purified alpha-glucosidase very rapidly hydrolized p-nitrophenyl alpha-D-glucopyranoside and sucrose. Maltose, maltotriose, isomaltose and isomaltotriose were hydrolized at slower rates, whereas beta-glucosides and polymeric alpha-glucans were not attacked. Other properties of the purified enzyme were as follows: Temperature optimum for catalysis = 39 +/- 1 degrees C; pH optimum = 6.8; molecular weight = 27,000 +/- 1000. alpha-Glucosidase is proposed to function in the endogenous metabolism of alpha-glucans provided extracellularly as carbon sources for growth of B. amyloliquefaciens.

Bacillus↗

PubMed1987

Developmentally regulated expression of temporally distinct beta-glucosidase isozymes in Dictyostelium discoideum.

During development of Dictyostelium discoideum, the cellular specific activity of beta-glucosidase increases before aggregation, declines to low levels during pseudoplasmodium formation, and increases rapidly during culmination. In addition, two electrophoretically distinct isozymes of beta-glucosidase are present at different times of development. Using enzyme-specific monoclonal antibodies, we have shown that changes in the level of enzyme specific activity are closely paralleled by changes in the relative rate of beta-glucosidase synthesis in vivo and by corresponding changes in the relative cellular concentration of functional beta-glucosidase mRNA. Thus, the developmental synthesis of beta-glucosidase is controlled at a pretranslational level. Furthermore, our experiments have demonstrated that both beta-glucosidase isozymes consist of a single subunit of identical molecular weight. This result is consistent with the previous finding that both isozymes are encoded by the same gene and suggests that the isozymes differ solely with respect to post-translational modification.

Dictyostelium↗

PubMed1999

Purification, partial amino acid sequence and structure of the product of raucaffricine-O-beta-D-glucosidase from plant cell cultures of Rauwolfia serpentina.

Plant cell suspension cultures of Rauwolfia produce within 1 week approximately 250 nkat/l of raucaffricine-O-beta-D-glucosidase. A five step procedure using anion exchange chromatography, chromatography on hydroxylapatite, gel filtration and FPLC-chromatography on Mono Q and Mono P delivered in a yield of 0.9% approximately 1200-fold enriched glucosidase. A short protocol employing DEAE sepharose, TSK 55 S gel chromatography and purification on Mono Q gave a 5% recovery of glucosidase which was 340-fold enriched. SDS-PAGE showed a Mr for the enzyme of 61 kDa. The enzyme is not glycosylated. Structural investigation of the enzyme product, vomilenine, demonstrated that the alkaloid exists in aqueous solutions in an equilibrium of 21(R)- and 21(S)-vomilenine in a ratio of 3.4:1. Proteolysis of the pure enzyme with endoproteinase Lys C revealed six peptide fragments with 6-24 amino acids which were sequenced. The two largest fragments showed sequences, of which the motif Val-Thr-Glu-Asn-Gly is typical for beta-glucosidases. Sequence alignment of these fragments demonstrated high homologies to linamarase from Manihot esculenta (81% identity) or to beta-glucosidase from Prunus avium (79% identity). Raucaffricine-O-beta-D-glucosidase seems to be a new member of the family 1 of glycosyl hydrolases.

Amino Acid Sequence↗

PubMed1989

Kinetic analysis of the interaction of alkyl glycosides with two human beta-glucosidases.

This paper addresses the similarities and differences in the topology of the catalytic centres of human liver cytosolic beta-glucosidase and placental lysosomal glucocerebrosidase, and utilizes well-documented reversible active-site-directed inhibitors. This comparative kinetic study was performed mainly to decipher the chemical and structural nature of the active site of the cytosolic beta-glucosidase, whose physiological function is unknown. Specifically, analysis of the effects of a family of alkyl beta-glucosides consistently displayed 100-250-fold lower inhibition constants with the cytosolic broad-specificity beta-glucosidase compared with the placental glucocerebrosidase; for example, with octyl beta-D-glucoside the Ki values were 10 microM and 1490 microM for the cytosolic and lysosomal beta-glucosidases respectively. Furthermore the higher affinity of the cytosolic beta-glucosidase than glucocerebrosidase for the amphipathic alkyl beta-D-glucosides was validated by the greater increase in the free energy of binding with increasing alkyl chain length [delta delta G0 (K,)/CH2: lysosomal enzyme, 2.01 kJ/mol (480 cal/mol); cytosolic enzyme, 3.05 kJ/mol (730 cal/mol)]. The implications of the presence of highly non-polar domains in the active site of the cytosolic beta-glucosidase are discussed with regard to its potential physiological substrates.

Binding Sites↗

PubMed1979

Genetics of type II glycogenosis: assignment of the human gene for acid alpha-glucosidase to chromosome 17.

We have studied somatic cell hybrids between thymidine kinase (EC 2.7.1.75) deficient mouse cells and human diploid fibroblasts for the expression of human acid alpha-glucosidase (EC 3.2.1.20). A deficiency in this enzyme is associated with the type II glycogenosis or Pompe disease. All 30 somatic cell hybrids selected in hypoxanthine/aminopterin/thymidine medium expressed human acid alpha-glucosidase and galactokinase (EC 2.7.1.6) and retained human chromosome 17; counterselection of the same hybrids in medium containing 5-bromodeoxyuridine resulted in the growth of hybrids that concordantly lost the expression of human acid alpha-glucosidase and galactokinase as well as human chromosome 17. Hybrids between thymidine kinase-deficient mouse cells and fibroblasts from a patient with Pompe disease that contained human chromosome 17 were found not to express human acid alpha-glucosidase. Because we have already shown that hybrids between mouse peritoneal macrophages and GM54VA simian virus 40-transformed human cells selectively retain human chromosome 17 and lose all other human chromosomes, we tested 13 independent mouse macrophage x GM54VA hybrid clones, including two that retained human chromosome 17 and no other human chromosomes, for the expression of human acid alpha-glucosidase and galactokinase. All 13 hybrid clones were found to express these human enzymes. Thus, we conclude that the gene coding for human acid alpha-glucosidase is located on human chromosome 17.

Animals↗

PubMed1980

Assay of the beta-glucosidase activity with natural labelled and artificial substrates in cultivated skin fibroblasts from homozygotes and heterozygotes with the Norrbottnian type of Gaucher disease.

Fibroblasts from 13 homozygotes and 27 obligate heterozygotes with the Norrbottnian type of Gaucher disease and 17 controls were cultivated and assayed with five beta-glucosidase methods, two with D-[glucose-U-14C] glucosylceramide and three with the artificial substrate 4-methylumbelliferyl-beta-glucoside. Two marker enzymes were assayed on the same cell samples, 4-methylumbelliferyl-beta-galactosidase and N-acetyl-beta-glucosaminidase. The beta-glucosidase activity of cultured fibroblasts, as measured with all five beta-glucosidase methods, was significantly lower (P < 0.001) for Gaucher homozygotes than heterozygotes. There was no overlap between fibroblasts from Gaucher homozygotes and the others with any of the beta-glucosidase methods used. The beta-glucosidase activity was also significantly lower (P < 0.001) for Gaucher heterozygotes than controls. However, none of the five beta-glucosidase assays differentiated between all Gaucher heterozygotes and controls, as several overlaps occurred in each assay.

Adolescent↗

PubMed1983

Presence of alpha-glucosidases in the male reproductive system of the rat and hormonal influences.

The use of a synthetic substrate (p-nitrophenyl-alpha-D-glucoside) to measure alpha-glucosidase activity has allowed us to demonstrate the presence of acid and neutral alpha-glucosidases in the reproductive organs of the male rat. Both enzymes increased in the epididymis, particularly in the caput segment, along with initiation of spermatogenesis at puberty; it then started decreasing after 12 weeks of life. Similar variations were not recorded in testis, prostate, and seminal vesicles. Castration led to a significant decrease of acid and neutral alpha-glucosidases in all accessory reproductive organs, but administration of testosterone proprionate (50 micrograms/day for 10 days) restored the enzyme activity to its original level. When estradiol-17 beta (5 mg) was administered simultaneously with testosterone (500 micrograms), the antagonistic effect of estradiol on testosterone was particularly evident on the levels of neutral alpha-glucosidases which reached the castration range, while the acid alpha-glucosidase remained unchanged in epididymis, prostate, and seminal vesicles. These results show that both acid and neutral alpha-glucosidases may be influenced by gonadal hormones in the male rat.

Animals↗

PubMed1982

On the origin of alpha-glucosidase in human urine.

The recent findings that alpha-glucosidase from human kidney was identical with one component (F1) of the alpha-glucosidases found in human urine suggested the idea that this enzyme might originate in the kidneys. The present study was performed to test this idea by immunological methods. Urine alpha-glucosidase F1 was isolated in the electrophoretically homogeneous state, and the antibody prepared in rabbits was purified by affinity chromatography after the antisera were fractionally precipitated with ammonium sulfate and chromatographed on diethylamino ethyl (DEAE)-cellulose. The staining of human kidney tissue sections was performed by the indirect method, using alpha-glucosidase F1 antibody and fluorescein-conjugated anti-rabbit immunoglobulin goat sera. The proximal convoluted portion (proximal tubules) with brush border and Henle's loops (late proximal) were stained clearly. Preincubation of intact antibody with purified antigen prevented specific staining of the proximal convoluted portion and Henle's loops. In contrast, all other tissues of kidney were stained less positively or negatively. These results indicate that alpha-glucosidase F1 originates in the kidney, and that glucosidase is specifically localized in the proximal convoluted portion and Henle's loops.

Adult↗

PubMedDate not supplied

Semi-solid-state fermentation of Eicchornia crassipes biomass as lignocellulosic biopolymer for cellulase and 3-glucosidase production by cocultivation of Aspergillus niger RK3 and Trichoderma reesei MTCC164.

An aquatic weed biomass, Eicchornia crassipes, present in abundance and leading to a threatening level of water pollution was used as substrate for cellulase and beta-glucosidase production using wild-type strain Aspergillus niger RK3 that was isolated from decomposing substrate. Alkali treatment of the biomass (10%) resulted in a 60-66% increase in endoglucanase, exoglucanase, and beta-glucosidase production by the A. niger RK3 strain in semi-solid-state fermentation. Similarly, the alkali-treated biomass led to a 45-54% increase in endo- and exoglucanase and a higher (98%) increase in beta-glucosidase production by Trichoderma reesei MTCC164 under similar conditions. However, the cocultivation of A. niger RK3 and T. reesei MTCC164 at a ratio of 3:1 showed a 20-24% increase in endo- and exoglucanase activities and about a 13% increase in the beta-glucosidase activity over the maximum enzymatic activities observed under single culture conditions. Multistep physical (ultraviolet) and chemical (N-methyl-N'-nitrosoguanidine, sodium azide, colchicine) mutagenesis of the A. niger RK3 strain resulted in a highly cellulolytic mutant, UNSC-442, having an increase of 136, 138, and 96% in endoglucanase, exoglucanase, and beta-glucosidase, activity, respectively. The cocultivation of mutant UNSC-442 along with T. reesei MTCC164 (at a ratio of 3:1) showed a further 10-11% increase in endo- and exoglucanase activities and a 29% increase in beta-glucosidase activity in semi-solid-state fermentation.

Aspergillus niger↗

PubMed1982

Soluble and membranous neutral beta-glucosidases.

Three distinct forms of beta-glucosidase were separated by Bio-Gel P-150 gel filtration from the 105,000 x g supernatant of liver, placenta and fibroblasts extracted in the presence of Cutscum and sodium taurocholate. Glucosylceramide beta-glucosidase was mostly particulate (more than 80%), had an apparent molecular weight of about 67,000 and exhibited a pH optimum of 5.9 with the natural substrate, glucosylceramide, and a pH optimum of 4.2 with the artificial substrate, 4-methylumbelliferyl beta-D-glucoside. This enzyme form was deficient in tissue specimens from patients with Gaucher disease. A soluble form with neutral pH optimum (6.2) was found to occur in high levels in liver and placenta but was relatively low in skin fibroblasts. This beta-glucosidase form had an apparent molecular weight of about 42,000 and was normal in the Gaucher tissues examined. Another neutral beta-glucosidase was found in the membranous fraction, it had a molecular weight greater than 150,000, cleaved 4-methylumbelliferyl beta-D-glucoside but not glucosylceramide, with an optimum pH of about 5.7. The membranous acidic and neutral forms could not be precipitated by antibodies to the soluble neutral beta-glucosidase. The three enzyme forms differed from one another by their heat inactivation profiles, the soluble neutral form was most labile, the membranous neutral form was most stable, and the acidic form with glucosylceramide beta-glucosidase activity had intermediate thermostability.

Antigens↗

PubMed1993

Inhibition of experimental metastasis by an alpha-glucosidase inhibitor, 1,6-epi-cyclophellitol.

Isolated from a culture filtrate of Phellinus sp., cyclophellitol is a specific inhibitor of beta-glucosidase, but unlike castanospermine, it does not inhibit experimental metastasis. However, its structural analogue, 1,6-epi-cyclophellitol, inhibited alpha-glucosidase as well as beta-glucosidase, and inhibited experimental metastasis. 1,6-Epi-cyclophellitol depressed alpha-glucosidase activity in cultured B16/F10 cells after 48 h of incubation. Preincubation of B16/F10 cells for 48 h with 1,6-epi-cyclophellitol inhibited invasion of the cells in a Boyden chamber assay at the doses effective in inhibiting alpha-glucosidase in situ. Pulmonary metastasis of B16/F10 cells in mice was inhibited by pretreatment of the cells with 1,6-epi-cyclophellitol in culture. The inhibitor reduced the collagen type I- and IV-mediated attachment of the cells, whereas it had no effect on laminin-mediated attachment. These results suggest that alpha-glucosidase in tumor cells is essential for the metastatic process through the cellular interaction with collagen type I and IV.

Animals↗

PubMedDate not supplied

Cloning and characterization of baker's yeast alpha-glucosidase: over-expression in a yeast strain devoid of vacuolar proteinases.

Two alpha-glucosidase (maltase) genes, designated GLUCPI and GLUCPII, have been cloned from an industrial strain of baker's yeast (Saccharomyces cerevisiae) by complementation of a maltase-negative mutant strain. The different genes were identified according to their alternatively expressed isoenzymes PI and PII in transformants after isoelectric focusing and activity staining in separated cell lysates. The gene encoding alpha-glucosidase PI (GLUCPI), which was not present in laboratory strains of S. carlsbergensis with a defined MAL1, 2, 3, 4 or 6 locus, was sequenced and compared with the recently published MAL6S gene. This comparison revealed single amino acid deviations at three positions in the predicted polypeptide sequence. In addition, the divergent promoter region of GLUCPI differed from MAL6S by a triple repeated 147-bp DNA segment. Maltose induction and glucose repression of alpha-glucosidase PI were not affected by the deletion of the repeated DNA segment. However, the absolute expression of alpha-glucosidase PI increased two- to four-fold. In addition, a two-fold increase in the maltase synthesis occurred when the cloned positive regulator gene MAL2-8ep was on the same plasmid. Furthermore, stability of the alpha-glucosidase in cultures in the stationary growth phase was greatly enhanced using a host strain lacking the proteinases A and B and the carboxypeptidases Y and S. Promoter trimming, MAL2-8cp stimulation and the use of a host strain deficient in four vacuolar proteinases resulted in alpha-glucosidase PI expression of about 13% of the soluble protein.

Amino Acid Sequence↗

PubMed2000

Overexpression, purification, and characterization of a barley alpha-glucosidase secreted by Pichia pastoris.

alpha-Glucosidases (EC 3.2.1.20) are recognized as important in starch degradation during cereal seed germination. A barley (Hordeum vulgare) alpha-glucosidase expressed in Pichia pastoris was cultured in flasks; however, the yield was low necessitating the use of multiple batches. Problems arose because of significant variation between batches. We solved these problems by switching to a fermentation system producing a sufficient quantity of a uniform sample. Here we present the expression and purification of a recombinant alpha-glucosidase grown under fermentation conditions. We also present the results of experiments to characterize the thermostability, pH optimum, and substrate specificity of the recombinant enzyme. The optimal pH for the hydrolysis of maltose by recombinant alpha-glucosidase is between 3.5 and 4.5. The thermostability of recombinant alpha-glucosidase was determined at pH 4, where activity is optimal, and at pH 5 and 6, which better mimic the conditions used to convert barley starch to fermentable sugars during industrial processing. The results indicate the enzyme is most thermolabile at pH 4. However, the enzyme is protected from heat inactivation at pH 4 by high concentrations of sucrose. The purified enzyme hydrolyzed maltose three times more rapidly than nigerose and 20 times more rapidly than trehalose and isomaltose. Concentrations of maltose greater than 20 mM inhibited maltose hydrolysis. This is the first report of substrate inhibition for any alpha-glucosidase. The results indicate that the only significant difference between the recombinant enzyme and the previously characterized barley isoforms was the V(max) for maltose hydrolysis.

Disaccharides↗

PubMed1987

Histochemical detection of alpha-D-glucosidases and their molecular forms with 5-Br-4-Cl-3-indoxyl-alpha-D-glucoside.

5-Br-4-Cl-3-Indoxyl-alpha-D-gluco(pyrano)side was found to be the most suitable synthetic substrate for the demonstration of alpha-D-glucosidases in situ. Using an azoindoxyl procedure with hexazotized pararosaniline or new fuchsine at pH 5 in freeze-dried celloidine-mounted cryostat sections acid alpha-D-glucosidase (EC 3.2.1.20) was shown for the first time in lysosomes of many cells of fetal and adult rat, mouse, guinea-pig, marmoset and human organs. At pH 6.5, in chloroform-acetone pretreated cryostat sections plasma membrane alpha-D-glucosidases were shown in the brush border of enterocytes of the small and large intestine, in the brush border of proximal renal tubule cells and in the stereocilia of the epididymal duct. In an indigogenic procedure with ferricyanide/ferrocyanide as redox catalysator plasma membrane alpha-D-glucosidases were depicted as well as with the azo-indoxyl method; the demonstration of the acid alpha-D-glucosidase was inferior to that achieved with the azo-indoxyl procedure. Using tetrazolium salts as capture reagent intracellular localization was unsatisfactory. In enterocytes, a localization in the Golgi apparatus was shown by the azo-indoxyl procedure only. Analytical isoelectric focusing revealed organ-dependent differences of plasma membrane and lysosomal alpha-D-glucosidases. Compared with the already existing methods the azo-indoxyl and indigogenic procedures are by far the most suitable techniques.

Animals↗

PubMed1997

Synthesis of isopropyl-1-thio-beta-D-glucopyranoside (IPTGlc), an inducer of Aspergillus niger B1 beta-glucosidase production.

Production of beta-glucosidase in Aspergillus niger B1 is subjected to catabolic repression by glucose. Aspergillus niger B1 grown on bran as a carbon source secreted beta-glucosidase. The maximum level of the enzyme was reached after 7 d of fermentation. Addition of 1% glucose to the medium suppressed beta-glucosidase production to undetectable levels. In this study, the organic synthesis of a potential inducer of beta-glucosidase production by A. niger B1's reported. Isopropyl-1-thio-beta-D-glucopyranoside (IPTGlc) was synthesized using a two-step organic synthesis protocol. The H-NMR data agreed with those reported previously for the galactoside analog. When IPTGlc was added 24 h after inoculation at a final concentration of 0.4 mM, similar levels of beta-glucosidase were reached 3 to 4 d earlier as compared to fermentation without IPTGlc induction. In practice, this may translate to a more efficient method of producing beta-glucosidase from this fungus.

Aspergillus niger↗