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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Biotechnological Potential of Agro-Industrial Wastes as a Carbon Source to Thermostable Polygalacturonase Production in <italic>Aspergillus niveus</italic></title><author><name sortKey="Maller, Alexandre" sort="Maller, Alexandre" uniqKey="Maller A" first="Alexandre" last="Maller">Alexandre Maller</name><affiliation><nlm:aff id="I1">Biochemistry and Immunology Department, Ribeirão Preto School of Medicine, São Paulo University, Avenue Bandeirantes, 3900, 14049-900 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Damasio, Andre Ricardo Lima" sort="Damasio, Andre Ricardo Lima" uniqKey="Damasio A" first="André Ricardo Lima" last="Damásio">André Ricardo Lima Damásio</name><affiliation><nlm:aff id="I1">Biochemistry and Immunology Department, Ribeirão Preto School of Medicine, São Paulo University, Avenue Bandeirantes, 3900, 14049-900 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Da Silva, Tony Marcio" sort="Da Silva, Tony Marcio" uniqKey="Da Silva T" first="Tony Marcio" last="Da Silva">Tony Marcio Da Silva</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Jorge, Joao Atilio" sort="Jorge, Joao Atilio" uniqKey="Jorge J" first="João Atílio" last="Jorge">João Atílio Jorge</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Terenzi, Hector Francisco" sort="Terenzi, Hector Francisco" uniqKey="Terenzi H" first="Héctor Francisco" last="Terenzi">Héctor Francisco Terenzi</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Polizeli, Maria De Lourdes Teixeira De Moraes" sort="Polizeli, Maria De Lourdes Teixeira De Moraes" uniqKey="Polizeli M" first="Maria De Lourdes Teixeira De Moraes" last="Polizeli">Maria De Lourdes Teixeira De Moraes Polizeli</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21837272</idno><idno type="pmc">3132474</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3132474</idno><idno type="RBID">PMC:3132474</idno><idno type="doi">10.4061/2011/289206</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000E83</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Biotechnological Potential of Agro-Industrial Wastes as a Carbon Source to Thermostable Polygalacturonase Production in <italic>Aspergillus niveus</italic></title><author><name sortKey="Maller, Alexandre" sort="Maller, Alexandre" uniqKey="Maller A" first="Alexandre" last="Maller">Alexandre Maller</name><affiliation><nlm:aff id="I1">Biochemistry and Immunology Department, Ribeirão Preto School of Medicine, São Paulo University, Avenue Bandeirantes, 3900, 14049-900 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Damasio, Andre Ricardo Lima" sort="Damasio, Andre Ricardo Lima" uniqKey="Damasio A" first="André Ricardo Lima" last="Damásio">André Ricardo Lima Damásio</name><affiliation><nlm:aff id="I1">Biochemistry and Immunology Department, Ribeirão Preto School of Medicine, São Paulo University, Avenue Bandeirantes, 3900, 14049-900 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Da Silva, Tony Marcio" sort="Da Silva, Tony Marcio" uniqKey="Da Silva T" first="Tony Marcio" last="Da Silva">Tony Marcio Da Silva</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Jorge, Joao Atilio" sort="Jorge, Joao Atilio" uniqKey="Jorge J" first="João Atílio" last="Jorge">João Atílio Jorge</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Terenzi, Hector Francisco" sort="Terenzi, Hector Francisco" uniqKey="Terenzi H" first="Héctor Francisco" last="Terenzi">Héctor Francisco Terenzi</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author><author><name sortKey="Polizeli, Maria De Lourdes Teixeira De Moraes" sort="Polizeli, Maria De Lourdes Teixeira De Moraes" uniqKey="Polizeli M" first="Maria De Lourdes Teixeira De Moraes" last="Polizeli">Maria De Lourdes Teixeira De Moraes Polizeli</name><affiliation><nlm:aff id="I2">Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</nlm:aff></affiliation></author></analytic><series><title level="j">Enzyme Research</title><idno type="ISSN">2090-0406</idno><idno type="eISSN">2090-0414</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Agro-industrial wastes are mainly composed of complex polysaccharides that might serve as nutrients for microbial growth and production of enzymes. The aim of this work was to study polygalacturonase (PG) production by <italic>Aspergillus niveus</italic> cultured on liquid or solid media supplemented with agro-industrial wastes. Submerged fermentation (SbmF) was tested using Czapeck media supplemented with 28 different carbon sources. Among these, orange peel was the best PG inducer. On the other hand, for solid state fermentation (SSF), lemon peel was the best inducer. By comparing SbmF with SSF, both supplemented with lemon peel, it was observed that PG levels were 4.4-fold higher under SSF. Maximum PG activity was observed at 55°C and pH 4.0. The enzyme was stable at 60°C for 90 min and at pH 3.0–5.0. The properties of this enzyme, produced on inexpensive fermentation substrates, were interesting and suggested several biotechnological applications.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Yadav, S" uniqKey="Yadav S">S Yadav</name></author><author><name sortKey="Yadav, Pk" uniqKey="Yadav P">PK Yadav</name></author><author><name sortKey="Yadav, D" uniqKey="Yadav D">D Yadav</name></author><author><name sortKey="Yadav, Kds" uniqKey="Yadav K">KDS Yadav</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Round, An" uniqKey="Round A">AN Round</name></author><author><name sortKey="Rigby, Nm" uniqKey="Rigby N">NM Rigby</name></author><author><name sortKey="Macdougall, Aj" uniqKey="Macdougall A">AJ MacDougall</name></author><author><name sortKey="Morris, Vj" uniqKey="Morris V">VJ Morris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hoondal, G" uniqKey="Hoondal 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Enzyme Res</journal-id><journal-id journal-id-type="publisher-id">ER</journal-id><journal-title-group><journal-title>Enzyme Research</journal-title></journal-title-group><issn pub-type="ppub">2090-0406</issn><issn pub-type="epub">2090-0414</issn><publisher><publisher-name>SAGE-Hindawi Access to Research</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21837272</article-id><article-id pub-id-type="pmc">3132474</article-id><article-id pub-id-type="doi">10.4061/2011/289206</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Biotechnological Potential of Agro-Industrial Wastes as a Carbon Source to Thermostable Polygalacturonase Production in <italic>Aspergillus niveus</italic></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Maller</surname><given-names>Alexandre</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Damásio</surname><given-names>André Ricardo Lima</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>da Silva</surname><given-names>Tony Marcio</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Jorge</surname><given-names>João Atílio</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Terenzi</surname><given-names>Héctor Francisco</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Polizeli</surname><given-names>Maria de Lourdes Teixeira de Moraes</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="I1"><sup>1</sup>Biochemistry and Immunology Department, Ribeirão Preto School of Medicine, São Paulo University, Avenue Bandeirantes, 3900, 14049-900 Ribeirão Preto, SP, Brazil</aff><aff id="I2"><sup>2</sup>Biology Department, Philosophy, Ribeirão Preto School of Philosophy, Sciences and Literature, São Paulo University, Avenue Bandeirantes, 3900, 14040-901 Ribeirão Preto, SP, Brazil</aff><author-notes><corresp id="cor1">*Maria de Lourdes Teixeira de Moraes Polizeli: <email>polizeli@ffclrp.usp.br</email></corresp><fn fn-type="other"><p>Academic Editor: Richard John Ward</p></fn></author-notes><pub-date pub-type="collection"><year>2011</year></pub-date><pub-date pub-type="epub"><day>20</day><month>6</month><year>2011</year></pub-date><volume>2011</volume><elocation-id>289206</elocation-id><history><date date-type="received"><day>27</day><month>10</month><year>2010</year></date><date date-type="rev-recd"><day>15</day><month>3</month><year>2011</year></date><date date-type="accepted"><day>23</day><month>4</month><year>2011</year></date></history><permissions><copyright-statement>Copyright © 2011 Alexandre Maller et al.</copyright-statement><copyright-year>2011</copyright-year><license license-type="open-access"><license-p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><abstract><p>Agro-industrial wastes are mainly composed of complex polysaccharides that might serve as nutrients for microbial growth and production of enzymes. The aim of this work was to study polygalacturonase (PG) production by <italic>Aspergillus niveus</italic> cultured on liquid or solid media supplemented with agro-industrial wastes. Submerged fermentation (SbmF) was tested using Czapeck media supplemented with 28 different carbon sources. Among these, orange peel was the best PG inducer. On the other hand, for solid state fermentation (SSF), lemon peel was the best inducer. By comparing SbmF with SSF, both supplemented with lemon peel, it was observed that PG levels were 4.4-fold higher under SSF. Maximum PG activity was observed at 55°C and pH 4.0. The enzyme was stable at 60°C for 90 min and at pH 3.0–5.0. The properties of this enzyme, produced on inexpensive fermentation substrates, were interesting and suggested several biotechnological applications.</p></abstract></article-meta></front><body><sec sec-type="section" id="sec1"><title>1. Introduction</title><p>Pectolytic enzymes are involved in the degradation of pectin, a structural component of the middle lamella and the primary cell walls of plants. Pectins are complex colloidal acidic polysaccharides that show a backbone of galacturonic acid residues with <italic>α</italic>-1,4-glycosidic linkages [<xref ref-type="bibr" rid="B1">1</xref>]. These molecules possess L-rhamnose, arabinose, galactose, and xylose in the side chains. Also, the carboxylic groups in the galacturonic acid chain are neutralized by different ions, as Na<sup>+</sup>, K<sup>+</sup>, and NH<sub>4</sub> <sup>+</sup> [<xref ref-type="bibr" rid="B2">2</xref>]. Pectins comprise a family of oligosaccharides and polysaccharides that have common features, but are extremely diverse in their fine structures. However, all pectins are rich in galacturonic acid (GalA) and they have at least 65% GalA. </p><p>Pectinolytic enzymes break down pectin or pectate by the hydrolysis of <italic>α</italic>-1,4-glycosidic linkages and they have varied biotechnological applications. The acidophilic pectinases have extensive applications in the manufacture of fruit juices and wine. They are used in apple juice preparation and clarification, to facilitate pressing and juice extraction. Moreover, pectic enzymes are used to reduce haze or gelling of grape juice in wine manufacture and to enhance the quality of cider apple varieties that are bitter, sweet, or sour [<xref ref-type="bibr" rid="B3">3</xref>, <xref ref-type="bibr" rid="B4">4</xref>]. The alkaline pectinase also has various industrial applications, such as wastewater treatment, paper manufacturing, oil extraction, coffee and tea fermentation, processing and degumming of many plant fibers [<xref ref-type="bibr" rid="B3">3</xref>].</p><p>Several fungal species are effective degraders of pectic substances, being able to produce high amounts of pectinolytic enzymes [<xref ref-type="bibr" rid="B1">1</xref>]. A novel strain of <italic>A. niveus</italic> was isolated from Brazilian soil, which produces high levels of several hydrolytic enzymes, such as xylanase [<xref ref-type="bibr" rid="B5">5</xref>, <xref ref-type="bibr" rid="B6">6</xref>] and amylases [<xref ref-type="bibr" rid="B7">7</xref>, <xref ref-type="bibr" rid="B8">8</xref>]. In this work, we demonstrated that this fungus also produced high polygalacturonase levels when grown on agricultural wastes, such as orange peel and passion fruit peel. This work leads to future biotechnological applications, and it also contributes to diminish the environmental pollution consequent of the accumulation of citric residues that are discarded in the environment.</p></sec><sec sec-type="section" id="sec2"><title>2. Materials and Methods</title><sec sec-type="subsection" id="sec2.1"><title>2.1. Organism and Growth Conditions</title><p><italic>Aspergillus niveus</italic> was isolated from <italic>Mangifera indica</italic> in our laboratory. The microorganism was identified and deposited in the culture collection of Pernambuco Federal University (PE, Brazil). The organism was maintained on slants of potato dextrose agar (PDA) medium covered with mineral oil, at 4°C. The fungus was incubated on PDA medium, at 30°C for 15 days previous to the cultivation and optimization experiments. After that, 5 × 10<sup>6</sup> conidia from these cultures were inoculated into 125-mL Erlenmeyer flasks containing 25 mL of liquid Czapeck medium [<xref ref-type="bibr" rid="B9">9</xref>] with 1.0% citric pectin Sigma (w/v) or other carbon sources as described in Results. The cultures were incubated at 40°C, under agitation (100 rpm) or under static conditions, for different periods, depending on the experiment. Other media were used to standardize the pectinolytic production, such as M-5 [<xref ref-type="bibr" rid="B10">10</xref>], Adams [<xref ref-type="bibr" rid="B11">11</xref>], Khanna [<xref ref-type="bibr" rid="B12">12</xref>], SR-Segato Rizzatti et al. [<xref ref-type="bibr" rid="B13">13</xref>] and Czapeck medium [<xref ref-type="bibr" rid="B9">9</xref>]. Cultures were filtered through Whatman no. 1 in a Buchner funnel. The filtrate was saved as a source of crude extracellular polygalacturonase. Micelial pads were ground with sea sand, at 4°C with ten vol. of cold 100 mM sodium acetate buffer, pH 6.0. After centrifugation (15,000 xg, 15 min, 4°C), the supernatant fraction was the source of crude intracellular enzyme.</p></sec><sec sec-type="subsection" id="sec2.2"><title>2.2. Culture Condition under SSF</title><p>The fungus was inoculated (5 × 10<sup>6</sup> conidia/mL) on SSF medium, composed by 2 g of different agro-industrial residues plus 4 mL of sterile distilled water. After the incubation period, the cultures were added of 50 mL of distilled water, maintained on ice and agitated for 30 min, after that, the extract fluid was separated from the solid residues as described in <xref ref-type="sec" rid="sec2.1">Section 2.1</xref>, and the filtrate was the source of crude extracellular polygalacturonase.</p></sec><sec sec-type="subsection" id="sec2.3"><title>2.3. Enzymatic Assays and Protein Determination</title><p>Polygalacturonase activity was assayed according to Miller [<xref ref-type="bibr" rid="B14">14</xref>]. The enzymatic assays were carried out with 50 <italic>μ</italic>L of enzyme and 1.0% polygalacturonic acid sodium salt from Sigma-Aldrich in 100 mM acetate buffer pH 4.0, as substrate. The reactions occurred at 60°C, for 5 min. A unit was defined as the amount of enzyme that releases 1 <italic>μ</italic>mol of reducing sugar per min under the assay conditions. Protein was assayed according to Lowry et al. [<xref ref-type="bibr" rid="B15">15</xref>], using bovine serum albumin as the standard. Total activity and total protein represent U/mL or mg/mL multiplied by total volume of culture filtrate.</p></sec><sec sec-type="subsection" id="sec2.4"><title>2.4. Reproducibility of the Results</title><p>All data are the mean of at least three independent experiments showing consistent results.</p></sec></sec><sec sec-type="section" id="sec3"><title>3. Results</title><sec sec-type="subsection" id="sec3.1"><title>3.1. Time-Course of Polygalacturonase Production</title><p>Regarding the nutritional composition of the culture medium, an experiment was carried out according to Cereia et al. [<xref ref-type="bibr" rid="B16">16</xref>]. <italic>A. niveus</italic> was preliminarily grown on a variety of liquid media (<xref ref-type="table" rid="tab1">Table 1</xref>). Among them, Czapeck medium was the best inducer for the PG production. </p><p>Then, the time-course of PG production was followed only with Czapeck medium added of 1% citrus pectin Sigma-Aldrich (w/v). The incubation occurred without agitation, up to 9 days, at 40°C, or under agitation for up to 5 days, at 40°C. Maximum growth occurred after four days without agitation (<xref ref-type="fig" rid="fig1">Figure 1(a)</xref>) and the PG production occurred after five days (<xref ref-type="fig" rid="fig1">Figure 1(b)</xref>).</p></sec><sec sec-type="subsection" id="sec3.2"><title>3.2. Effect of Carbon Sources on Growth and Enzymatic Production on SbmF and SSF</title><p>The effect of the carbon sources on SbmF was studied by supplementing the Czapeck medium with 28 carbohydrates and/or agro-industrial wastes (<xref ref-type="table" rid="tab2">Table 2</xref>). The cultures were incubated under agitation for 5 days and the fungal growth was expressed as total protein. The best source for PG production activity was orange peel, which was 21-fold higher than the basal activity in medium supplemented by glucose. Another agro-industrial residue tested was passion fruit peel, which resulted in PG levels 19-fold higher than the one in glucose-medium. Furthermore, lemon peel, apple peel, gum guar, commercial mate herb (<italic>Illex paraguariensis</italic>), and corncob were also tested and contributed to produce high PG activity from <italic>A. niveus</italic>. Sigma-Aldrich, CPKelco 8003, and Vetec citrus pectins led to about 19-fold increase in PG activity in relation to that attained on glucose-containing media. Pectins from different origins induced lower PG levels as well as polypectate acid salt sodium and monogalacturonic acid that were poor inducers. </p><p>Polygalacturonase production on SSF was studied by incubating the fungus with 8 different agro-industrial residues (<xref ref-type="table" rid="tab3">Table 3</xref>) for 7 days. Under this condition, lemon peel was the best inducer of PG activity. Besides, passion fruit peel was an interesting inducer showing the second best level. The other residues tested showed about half of the activity of the carbon sources previously mentioned. </p></sec><sec sec-type="subsection" id="sec3.3"><title>3.3. Biochemical Characterization of Polygalacturonase Activity</title><p>The enzyme used to biochemical characterization was the extracellular PG produced in medium supplemented with Sigma-Aldrich citrus pectin, because it showed elevated activity and few contaminants. The optima of temperature and pH were 55°C and the pH range of 3.0–4.5 (Figures <xref ref-type="fig" rid="fig2">2(a)</xref> and <xref ref-type="fig" rid="fig2">2(b)</xref>). The enzyme retained 91% of the activity after 90 min at 60°C; higher temperatures severely inactivated the enzyme (<xref ref-type="fig" rid="fig2">Figure 2(c)</xref>). PG activity remained stable after 24 h at 4–6°C at the pH range of 3.0–5.0, with a decrease of 15% at pH 5.5 and 91% at pH 8.0 (<xref ref-type="fig" rid="fig2">Figure 2(d)</xref>).</p><p>The effect of different salts and EDTA (1 and 10 mM, final concentration) on PG activity is shown in <xref ref-type="table" rid="tab4">Table 4</xref>. EDTA and Mn<sup>2+</sup> generated a slight increase in the enzymatic activity. However, 10 mM Hg<sup>2+</sup>, Ba<sup>2+</sup>, and Cu<sup>2+</sup> inhibited 96, 61, and 52% of the PG activity, respectively.</p></sec></sec><sec sec-type="section" id="sec4"><title>4. Discussion</title><p><italic>Aspergillus niveus</italic> turned out to be a good pectinase producer in cultures grown with agro-industrial residues. It is very convenient to use such residues to produce the enzyme in industrial scale, once their use reduces costs and aggregates value to the organic material, bringing benefits to the environment as well as the industry. When grown in Czapeck medium, the fungus had maximum PG production after 5 days. Patil and Dayanand [<xref ref-type="bibr" rid="B17">17</xref>] and Friedrich et al. [<xref ref-type="bibr" rid="B18">18</xref>] described similar period of time for pectinase production by different strains of <italic>Aspergillus niger</italic> in submerged cultures. The present study demonstrated that fruit peels, especially orange peels, considerably stimulated the production of PG under SbmF. However, Niture and Pant [<xref ref-type="bibr" rid="B19">19</xref>] described that orange peel induced elevated levels of PG II in <italic>Fusarium moniliforme</italic> grown in semisolid medium. Besides, our results showed that PG production by <italic>A. niveus</italic> was better under SSF than under SbmF, considering the same carbon source. The PG production with rice straw was 9.1-fold higher under SSF than in SbmF, followed by lemon peel and wheat bran (4.4-fold), corn cob (3.9-fold), passion fruit (3.1-fold), sugar cane bagasse (2.9-fold), orange peel (1.5-fold), and apple peel (1.3-fold). These results suggested that the high enzymatic production is due to a close contact of the microorganism with the carbon source, observed in SSF.</p><p><italic>A. niveus</italic> is a thermotolerant fungus [<xref ref-type="bibr" rid="B20">20</xref>]; so, the PG secreted was quite active and stable at 60°C. Mohamed et al. [<xref ref-type="bibr" rid="B21">21</xref>] described a PG with optimum activity at 40°C. Kashyap et al. [<xref ref-type="bibr" rid="B22">22</xref>] and Moyo et al. [<xref ref-type="bibr" rid="B23">23</xref>] describe the maximum temperature of 50°C for the PG of<italic> A. niger </italic>and <italic>Kluyveromyces wickerhamii, </italic>respectively. The optimum temperature for PG from <italic>Bacillus</italic> sp. [<xref ref-type="bibr" rid="B4">4</xref>], <italic>Trichoderma harzianum</italic> [<xref ref-type="bibr" rid="B24">24</xref>], <italic>T. reesei </italic>[<xref ref-type="bibr" rid="B21">21</xref>], and <italic>A. niger</italic> [<xref ref-type="bibr" rid="B25">25</xref>] was about 40 and 50°C. </p><p>The <italic>A. niveus</italic> PG was stable for 90 min at 60°C. Mohamed et al. [<xref ref-type="bibr" rid="B24">24</xref>] describe that the PG of <italic>Trichoderma harzianum</italic> was stable for 30 min at 60°C. Thus, the PG from <italic>A. niveus </italic>may be advantageous for the industrial processes of candy, syrups, juice, and drink production.</p><p>PG activity was predominantly acidic, presenting two plateaus (pH range of 3–4.5 and 5–6.5, suggesting more than one enzymatic form). For <italic>A. niger</italic> [<xref ref-type="bibr" rid="B24">24</xref>] and <italic>Fusarium moniliforme </italic>[<xref ref-type="bibr" rid="B18">18</xref>], the maximum PG activity occurred at pH 5.0, and for <italic>T</italic>. <italic>reesei </italic>PGs at pH 4.5 and 4.2 [<xref ref-type="bibr" rid="B24">24</xref>]. The enzyme from <italic>A. niveus </italic>was stable in a pH range of 3.0–5.0, for 24 h at 4–6°C. The PG from <italic>T</italic>.<italic> harzianum</italic> [<xref ref-type="bibr" rid="B24">24</xref>] was stable at pH 5.0, and PG from <italic>A. fumigatus</italic> [<xref ref-type="bibr" rid="B3">3</xref>] was stable in a pH range of 3.0–9.0. Kobayashi et al. [<xref ref-type="bibr" rid="B26">26</xref>] demonstrated that PG from <italic>Bacillus</italic> sp. was stable at pH 6.0 and 12.0 at 30°C for 1 h. </p><p>EDTA and Mn<sup>2+</sup> increased the enzymatic activity of the PG from<italic> A. niveus</italic>, and Hg<sup>2+</sup>, Ba<sup>2+</sup>, and Cu<sup>2+</sup> inhibited it. The effect of Hg<sup>2+</sup> suggested the presence of SH groups on the protein, which was a covalent bound with this metal turning the three-dimensional structure unstable and decreasing its enzymatic activity. PGII from <italic>T. harzianum</italic> [<xref ref-type="bibr" rid="B24">24</xref>] was totality inhibited by 1mM Mn<sup>2+</sup> and Co<sup>2+</sup>. The activity of <italic>Sporotrichum thermophile Apinis</italic> PG was stimulated by Fe<sup>2+</sup> and Mn<sup>2+</sup> both at 1 and 5 mM, while Ca<sup>2+</sup> and Cu<sup>2+</sup> stimulated only at 1 mM and 5 mM. Mg<sup>2+</sup> strongly inhibited enzyme activity [<xref ref-type="bibr" rid="B27">27</xref>]. The PG of Bacillus MG-cp-2 was stimulated by Ca<sup>2+</sup> [<xref ref-type="bibr" rid="B4">4</xref>]. </p><p>In conclusion, agro-industrial residues, such as orange and lemon peel, induce high levels of a thermostable acid PG by <italic>A. niveus.</italic> Finally, the use of these residues on industrial enzymatic production would aggregate value to waste and would reduce the environmental pollution.</p></sec></body><back><ack><title>Acknowledgments</title><p>This work was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) and Conselho de Desenvolvimento Científico e Tecnológico (CNPq). João Atīlio Jorge and Maria de Lourdes Teixeira de Moraes Polizeli are Research Fellows of CNPq. Alexandre Maller; André Ricardo Lima Damásio; Tony Marcio da Silva were recipients of FAPESP Fellowship. 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publication-type="journal"><person-group person-group-type="author"><name><surname>Kaur</surname><given-names>G</given-names></name><name><surname>Kumar</surname><given-names>S</given-names></name><name><surname>Satyanarayana</surname><given-names>T</given-names></name></person-group><article-title>Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould <italic>Sporotrichum thermophile Apinis</italic></article-title><source><italic>Bioresource Technology</italic></source><year>2004</year><volume>94</volume><issue>3</issue><fpage>239</fpage><lpage>243</lpage><pub-id pub-id-type="pmid">15182829</pub-id></element-citation></ref></ref-list></back><floats-group><fig id="fig1" position="float"><label>Figure 1</label><caption><p>Time course of <italic>A. niveus</italic> cultivation. (a) Growth, (b) PG production, (■) static condition, (●) agitation condition.</p></caption><graphic xlink:href="ER2011-289206.001"></graphic></fig><fig id="fig2" position="float"><label>Figure 2</label><caption><p>Biochemical characterization of the PGs produced by <italic>A. niveus</italic>. (a) Effect of the temperature; (b) pH influence, (c) thermal stability, (d) pH stability, (■) 60°C; (●) 65°C; (▲) 70°C.</p></caption><graphic xlink:href="ER2011-289206.002"></graphic></fig><table-wrap id="tab1" position="float"><label>Table 1</label><caption><p>Effect of liquid media on growth and PG activity of <italic>A. niveus. </italic></p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Media</th><th align="center" rowspan="1" colspan="1">Relative growth (%)</th><th align="center" rowspan="1" colspan="1">Relative activity (%)</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">M-5</td><td align="center" rowspan="1" colspan="1">24 ± 0.4</td><td align="center" rowspan="1" colspan="1">32 ± 0.8</td></tr><tr><td align="left" rowspan="1" colspan="1">Adams</td><td align="center" rowspan="1" colspan="1">100 ± 0.3</td><td align="center" rowspan="1" colspan="1">62 ± 0.4</td></tr><tr><td align="left" rowspan="1" colspan="1">Khanna</td><td align="center" rowspan="1" colspan="1">6 ± 0.1</td><td align="center" rowspan="1" colspan="1">18 ± 1.7</td></tr><tr><td align="left" rowspan="1" colspan="1">SR</td><td align="center" rowspan="1" colspan="1">27 ± 0.4</td><td align="center" rowspan="1" colspan="1">33 ± 1.3</td></tr><tr><td align="left" rowspan="1" colspan="1">Czapeck</td><td align="center" rowspan="1" colspan="1">34 ± 0.4</td><td align="center" rowspan="1" colspan="1">100 ± 1.7</td></tr></tbody></table><table-wrap-foot><fn><p><italic>A. niveus</italic> was grown in 1% citric pectin media, for 3 days at 40°C.</p></fn></table-wrap-foot></table-wrap><table-wrap id="tab2" position="float"><label>Table 2</label><caption><p>Effect of different carbon sources on the production of PG from <italic>A. niveus </italic>under SbmF.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Source</th><th align="center" rowspan="1" colspan="1">Growth <break></break>(mg total of protein)</th><th align="center" rowspan="1" colspan="1">Activity <break></break>(U total)</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">Sigma-Aldrich Citrus Pectin</td><td align="center" rowspan="1" colspan="1">1.9 ± 0.07</td><td align="center" rowspan="1" colspan="1">319 ± 3</td></tr><tr><td align="left" rowspan="1" colspan="1">None</td><td align="center" rowspan="1" colspan="1">0.1 ± 0.06</td><td align="center" rowspan="1" colspan="1">36 ± 3</td></tr><tr><td align="left" rowspan="1" colspan="1">Glucose</td><td align="center" rowspan="1" colspan="1">0.1 ± 0.04</td><td align="center" rowspan="1" colspan="1">16 ± 2</td></tr><tr><td align="left" rowspan="1" colspan="1">Monogalacturonic acid</td><td align="center" rowspan="1" colspan="1">0.1 ± 0.05</td><td align="center" rowspan="1" colspan="1">102 ± 5</td></tr><tr><td align="left" rowspan="1" colspan="1">Polygalacturonic acid</td><td align="center" rowspan="1" colspan="1">0.2 ± 0.08</td><td align="center" rowspan="1" colspan="1">124 ± 4</td></tr><tr><td align="left" rowspan="1" colspan="1">7128 Citrus Pectin*</td><td align="center" rowspan="1" colspan="1">2.5 ± 0.06</td><td align="center" rowspan="1" colspan="1">286 ± 2</td></tr><tr><td align="left" rowspan="1" colspan="1">USP-B Citrus Pectin*</td><td align="center" rowspan="1" colspan="1">2.5 ± 0.07</td><td align="center" rowspan="1" colspan="1">274 ± 4</td></tr><tr><td align="left" rowspan="1" colspan="1">JMH6 Citrus Pectin*</td><td align="center" rowspan="1" colspan="1">2.5 ± 0.09</td><td align="center" rowspan="1" colspan="1">236 ± 4</td></tr><tr><td align="left" rowspan="1" colspan="1">GENU 8001 Citrus Pectin*</td><td align="center" rowspan="1" colspan="1">2.2 ± 0.08</td><td align="center" rowspan="1" colspan="1">268 ± 3</td></tr><tr><td align="left" rowspan="1" colspan="1">GEN 8003 Citrus Pectin*</td><td align="center" rowspan="1" colspan="1">2.6 ± 0.04</td><td align="center" rowspan="1" colspan="1">315 ± 3</td></tr><tr><td align="left" rowspan="1" colspan="1">Sucrose</td><td align="center" rowspan="1" colspan="1">3.8 ± 0.05</td><td align="center" rowspan="1" colspan="1">197 ± 4</td></tr><tr><td align="left" rowspan="1" colspan="1">Vetec Citrus Pectin</td><td align="center" rowspan="1" colspan="1">1.7 ± 0.09</td><td align="center" rowspan="1" colspan="1">307 ± 5</td></tr><tr><td align="left" rowspan="1" colspan="1">Galactose</td><td align="center" rowspan="1" colspan="1">3.1 ± 0.10</td><td align="center" rowspan="1" colspan="1">26 ± 2</td></tr><tr><td align="left" rowspan="1" colspan="1">Trehalose</td><td align="center" rowspan="1" colspan="1">2.6 ± 0.05</td><td align="center" rowspan="1" colspan="1">67 ± 3</td></tr><tr><td align="left" rowspan="1" colspan="1">Raffinose</td><td align="center" rowspan="1" colspan="1">2.7 ± 0.04</td><td align="center" rowspan="1" colspan="1">60 ± 2</td></tr><tr><td align="left" rowspan="1" colspan="1">Arabinose</td><td align="center" rowspan="1" colspan="1">3.8 ± 0.04</td><td align="center" rowspan="1" colspan="1">172 ± 4</td></tr><tr><td align="left" rowspan="1" colspan="1">Penetrose</td><td align="center" rowspan="1" colspan="1">5.2 ± 0.07</td><td align="center" rowspan="1" colspan="1">170 ± 3</td></tr><tr><td align="left" rowspan="1" colspan="1">Gum guar</td><td align="center" rowspan="1" colspan="1">3.7 ± 0.11</td><td align="center" rowspan="1" colspan="1">244 ± 2</td></tr><tr><td align="left" rowspan="1" colspan="1">Apple peel (<italic>Malus domestica</italic>)</td><td align="center" rowspan="1" colspan="1">4.5 ± 0.09</td><td align="center" rowspan="1" colspan="1">248 ± 7</td></tr><tr><td align="left" rowspan="1" colspan="1">Orange peel (<italic>Citrus sinensis</italic>)</td><td align="center" rowspan="1" colspan="1">2.4 ± 0.10</td><td align="center" rowspan="1" colspan="1">335 ± 9</td></tr><tr><td align="left" rowspan="1" colspan="1">Lemon peel (<italic>Citrus latifolia</italic>)</td><td align="center" rowspan="1" colspan="1">3.1 ± 0.12</td><td align="center" rowspan="1" colspan="1">300 ± 8</td></tr><tr><td align="left" rowspan="1" colspan="1">Passion fruit peel (<italic>Passiflora edulis</italic>)</td><td align="center" rowspan="1" colspan="1">3.6 ± 0.11</td><td align="center" rowspan="1" colspan="1">313 ± 6</td></tr><tr><td align="left" rowspan="1" colspan="1">commercial mate herb (<italic>Illex paraguariensis</italic>)</td><td align="center" rowspan="1" colspan="1">4.9 ± 0.09</td><td align="center" rowspan="1" colspan="1">136 ± 7</td></tr><tr><td align="left" rowspan="1" colspan="1">Rice straw (<italic>Oryza sativa</italic>)</td><td align="center" rowspan="1" colspan="1">1.0 ± 0.04</td><td align="center" rowspan="1" colspan="1">35 ± 4</td></tr><tr><td align="left" rowspan="1" colspan="1">Sugar cane bagasse (<italic>Saccharum officinarum</italic>)</td><td align="center" rowspan="1" colspan="1">1.6 ± 0.07</td><td align="center" rowspan="1" colspan="1">95 ± 6</td></tr><tr><td align="left" rowspan="1" colspan="1">Corn cob (<italic>Zea mays</italic>)</td><td align="center" rowspan="1" colspan="1">1.2 ± 0.03</td><td align="center" rowspan="1" colspan="1">105 ± 8</td></tr><tr><td align="left" rowspan="1" colspan="1">Wheat bran (<italic>Triticum aestivum</italic>)</td><td align="center" rowspan="1" colspan="1">3.1 ± 0.13</td><td align="center" rowspan="1" colspan="1">92 ± 5</td></tr><tr><td align="left" rowspan="1" colspan="1">Soya bran (<italic>Glycine max</italic>)</td><td align="center" rowspan="1" colspan="1">3.3 ± 0.10</td><td align="center" rowspan="1" colspan="1">73 ± 4</td></tr></tbody></table><table-wrap-foot><fn><p>* FROM CPKelco Brasil S/A.</p></fn></table-wrap-foot></table-wrap><table-wrap id="tab3" position="float"><label>Table 3</label><caption><p>Effect of different carbon sources on the production of PG from <italic>A. niveus </italic>under SSF.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Source</th><th align="center" rowspan="1" colspan="1">Growth <break></break>(mg total of protein)</th><th align="center" rowspan="1" colspan="1">Activity<break></break>(U total)</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">Orange peel (<italic>Citrus sinensis</italic>)</td><td align="center" rowspan="1" colspan="1">46 ± 2.9</td><td align="center" rowspan="1" colspan="1">495 ± 33</td></tr><tr><td align="left" rowspan="1" colspan="1">Lemon peel (<italic>Citrus latifolia</italic>)</td><td align="center" rowspan="1" colspan="1">39 ± 1.5</td><td align="center" rowspan="1" colspan="1">1324 ± 57</td></tr><tr><td align="left" rowspan="1" colspan="1">Passion fruit peel (<italic>Passiflora edulis</italic>)</td><td align="center" rowspan="1" colspan="1">42 ± 7.3</td><td align="center" rowspan="1" colspan="1">960 ± 15</td></tr><tr><td align="left" rowspan="1" colspan="1">Apple peel (<italic>Malus domestica</italic>)</td><td align="center" rowspan="1" colspan="1">42 ± 2.4</td><td align="center" rowspan="1" colspan="1">311 ± 36</td></tr><tr><td align="left" rowspan="1" colspan="1">Rice straw (<italic>Oryza sativa</italic>)</td><td align="center" rowspan="1" colspan="1">5 ± 0.1</td><td align="center" rowspan="1" colspan="1">318 ± 27</td></tr><tr><td align="left" rowspan="1" colspan="1">Wheat bran (<italic>Triticum aestivum</italic>)</td><td align="center" rowspan="1" colspan="1">26 ± 1.4</td><td align="center" rowspan="1" colspan="1">407 ± 25</td></tr><tr><td align="left" rowspan="1" colspan="1">Corn cob (<italic>Zea mays</italic>)</td><td align="center" rowspan="1" colspan="1">14 ± 0.5</td><td align="center" rowspan="1" colspan="1">416 ± 1</td></tr><tr><td align="left" rowspan="1" colspan="1">Sugar cane bagasse (<italic>Saccharum officinarum</italic>)</td><td align="center" rowspan="1" colspan="1">5 ± 0.1</td><td align="center" rowspan="1" colspan="1">272 ± 10</td></tr></tbody></table></table-wrap><table-wrap id="tab4" position="float"><label>Table 4</label><caption><p>Effect of metal ions and EDTA on the activity of the PG produced by <italic>A. niveus. </italic></p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="2" colspan="1">Compound</th><th align="center" colspan="2" rowspan="1">Relative activity (%)</th></tr><tr><th align="center" rowspan="1" colspan="1">1 mM</th><th align="center" rowspan="1" colspan="1">10 mM</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">None</td><td align="center" rowspan="1" colspan="1">100 ± 2.1</td><td align="center" rowspan="1" colspan="1">100 ± 1.3</td></tr><tr><td align="left" rowspan="1" colspan="1">Hg<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">59 ± 2.9</td><td align="center" rowspan="1" colspan="1">4 ± 1.0</td></tr><tr><td align="left" rowspan="1" colspan="1">NH<sub>4</sub> <sup>+</sup></td><td align="center" rowspan="1" colspan="1">87 ± 3.0</td><td align="center" rowspan="1" colspan="1">87 ± 2.1</td></tr><tr><td align="left" rowspan="1" colspan="1">Ca<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">97 ± 2.8</td><td align="center" rowspan="1" colspan="1">78 ± 2.5</td></tr><tr><td align="left" rowspan="1" colspan="1">Zn<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">87 ± 2.6</td><td align="center" rowspan="1" colspan="1">75 ± 2.2</td></tr><tr><td align="left" rowspan="1" colspan="1">Ba<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">101 ± 1.3</td><td align="center" rowspan="1" colspan="1">39 ± 2.8</td></tr><tr><td align="left" rowspan="1" colspan="1">Cu<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">60 ± 1.9</td><td align="center" rowspan="1" colspan="1">48 ± 2.4</td></tr><tr><td align="left" rowspan="1" colspan="1">Na<sup>+</sup></td><td align="center" rowspan="1" colspan="1">95 ± 2.8</td><td align="center" rowspan="1" colspan="1">93 ± 2.0</td></tr><tr><td align="left" rowspan="1" colspan="1">Mn<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">117 ± 1.4</td><td align="center" rowspan="1" colspan="1">113 ± 3.2</td></tr><tr><td align="left" rowspan="1" colspan="1">Mg<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">72 ± 2.9</td><td align="center" rowspan="1" colspan="1">92 ± 2.9</td></tr><tr><td align="left" rowspan="1" colspan="1">Al<sup>2+</sup></td><td align="center" rowspan="1" colspan="1">98 ± 2.3</td><td align="center" rowspan="1" colspan="1">93 ± 2.1</td></tr><tr><td align="left" rowspan="1" colspan="1">EDTA</td><td align="center" rowspan="1" colspan="1">110 ± 3.2</td><td align="center" rowspan="1" colspan="1">94 ± 3.3</td></tr></tbody></table></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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