Abstract
Stachybotrys microspora is a filamentous fungus characterized by the secretion of multiple β-glucosidases. The production of these enzymes was studied under culture with variable carbon sources. The highest activity was produced on glucose (0.66 U ml−1) whereas galactose, lactose, cellobiose, Avicel cellulose, carboxymethylcellulose (CMC), wheat bran and gruel allowed intermediate production levels ranging between 0.08 and 0.48 U ml−1. The zymogram analysis showed that complex sugars such as Avicel cellulose and CMC induced the expression of several β-glucosidases whereas all tested simple sugars (mono and disaccharides) induced the expression of one single β-glucosidase, each time different. The most efficient β-glucosidase named bglG was produced on glucose which continues to be, at the same time, its strong inhibitor. The bglG N-terminal sequence confirmed that it is a novel β-glucosidase. According to its large molecular weight, this enzyme was assumed to belong to family 3 of β-glucosidases. RT-PCR analysis showed that family 3 expressions were induced on glucose while those of family 1 were repressed. Finally, with the use of different combinations of glucose and various carbon sources at different ratio, we showed that such sources direct the differential expression of β-glucosidases in S. microspora since our strain co-produced the β-glucosidases corresponding to each carbon source.






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Amouri B, Gargouri A (2006) Characterization of a novel β-glucosidase from a Stachybotrys strain. Biochem Eng J 32:191–197
Aro N, Ilme′n M, Saloheimo A, Penttila M (2003) ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression. Appl Environ Microbiol: 56–65
Ayers AR, Ayers SB, Eriksson KE (1978) Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum. Eur J Biochem 90:171–181
Bao W, Usha SN, Renganathan V (1993) Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium. Arch Biochem Biophys 300:705–713
Brini F, Saibi W, Amara I, Gargouri A, Masmoudi K, Hanin M (2010) Wheat dehydrin DHN-5 exerts a heat-protective effect on β-glucosidase and glucose oxidase activities. Biosci Biotechnol Biochem 74:1050–1054
Eriksson KE (1978) Enzyme mechanisms involved in cellulose hydrolysis by the white-rot fungus Sporotrichum pulverulentum. Biotechnol Bioeng 70:317–332
Esen A (1993) Beta-glucosidases. Biochem Mol Biol (Acs Symposium Series 533)
Laemmli UK, Favre M (1973) Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol 80:575–599
Makoto Y, Kiyohiko I, Rie K, Katsumi A, Masahiro S (2004) Differential transcription of b-glucosidase and cellobiose dehydrogenase genes in cellulose degradation by the basidiomycete Phanerochaete chrysosporium. FEMS Microbiol Lett 235:177–182
Mandels M, Reese E (1957) Induction of cellulase in Trichoderma viride as influenced by carbon sources and metals. J Bacterial 73:269–278
Nakata T, Miyafuji H, Saka S (2006) Bioethanol from cellulose with supercritical water treatment followed by enzymatic hydrolysis. Appl Biochem Biotech 130:476–485
Pérez M, Muñoz FJ, Muñoz E, Fernández M, Sinisterra JV, Hernáiz MJ (2008) Synthesis of novel glycoconjugates and evaluation as inhibitors against β-glucosidase from almond. J Mol Catal B Enzymatic 52–53:153–157
Premkumar L, Sawkar AR, Boldin-Adamsky S, Toker L, Silman I, Futerman AH, Sussman JL (2005) X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease. J Biol Chem 280:23815–23819
Saibi W, Amouri B, Gargouri A (2007) Purification and biochemical characterization of a transglucosilating β-glucosidase of Stachybotrys strain. Appl Microbiol Biotechnol 77:293–300
Sehnem NT, de Bittencourt LR, Camassola M, Dillon AJ (2006) Cellulase production by Penicillium echinulatum on lactose. Appl Microbiol Biotechnol 72:163–167
Shewale JG (1982) b-Glucosidase: its role in cellulase synthesis and hydrolysis of cellulose. Int J Biochem 14:435–443
Smaali MI, Michaud N, Marzouki N, Legoy MD, Maugard T (2004) Comparison of two beta-glucosidases for the enzymatic synthesis of beta-(1–6)-beta-(1–3)-gluco-oligosaccharides. Biotechnol Lett 26:675–679
Sternberg D, Vijayakumar P, Reese ET (1977) β-Glucosidase: microbial production and effect on enzymatic hydrolysis of cellulose. Can J Microbiol 23:139–147
Suto M, Tomita F (2001) Induction and catabolite repression mechanisms of cellulase in fungi. J Biosci Bioeng 92:305–311
Takeshi T, Kiyohiko I, Shinya F, Masahiro S (2008) Role of subsite R1 residues in pH dependence and catalytic activity of the glycoside hydrolase family 1 b-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium. Biotechnol Bioeng 99:1295–1302
Tokuhiro K, Ishida N, Kondo A, Takahashi H (2008) Lactic fermentation of cellobiose by a yeast strain displaying β-glucosidase on the cell surface. Appl Microbiol Biotechnol 79:481–488
Yu S, Yan Z, Tao M, Xiaoming B, Fengguang D, Guoqiang Z, Yinbo Q (2008) Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing β-glucosidase. Bioresour Technol 99:5099–5103
Acknowledgments
This work is dedicated to the memory of Pr. Mokhtar Trifi. We thank Khmaies Benhaj Hafedh Belghith and Fatma Abdeljalil for their help in manuscript correction. Mosbeh Dardouri is thanked for his technical help. This work was supported by grants from the Ministry of Higher Education and Scientific Research, Tunisia.
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Saibi, W., Abdeljalil, S. & Gargouri, A. Carbon source directs the differential expression of β-glucosidases in Stachybotrys microspora . World J Microbiol Biotechnol 27, 1765–1774 (2011). https://doi.org/10.1007/s11274-010-0634-x
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DOI: https://doi.org/10.1007/s11274-010-0634-x


