Pectinase

<h2 id="pectinase-in-nature">Pectinase in nature</h2>
<p>Pectinase enzymes used today are naturally produced by fungi and yeasts (50%), insects, bacteria and microbes (35%) and various plants (15%),<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> but cannot be synthesized by animal or human cells.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> In plants, pectinase enzymes hydrolyze pectin that is found in the cell wall, allowing for new growth and changes to be made. Similarly to their role in plants, pectinases break down pectin during the developmental stage of fungi.
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<h2 id="characterizations">Characterizations</h2>
<p>Pectinase enzymes are classified based on how their enzymatic reaction proceeds with various pectic substances (through transelimination or hydrolysis), the preferred substrate (pectin, pectic acid or oligo-n-galacturonate) and if the cleavage that occurs is random or end-wise.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a><a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a>
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<h2 id="reaction-pathway">Reaction pathway</h2>
<p>Pectinases depolymerise <a href="/facts/Pectin/nQF6T0Q7">pectin</a> through <a href="/facts/Hydrolysis/JTvwIHPs">hydrolysis</a>, trans-elimination and deesterification reaction processes, breaking down the ester bond that holds together the carboxyl and methyl groups in pectin.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a>
</p><p>Endo-polygalacturonase progresses through a reaction along the following pathway:<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a>
</p><p>(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m
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<h2 id="crystal-structures">Crystal structures</h2>
<p>All pectinase enzyme structures include a prism-shaped right-handed cylinder made up of seven to nine parallel β-helices. The three parallel β-helices that create the prism shape of the structure are referred to as PB1, PB2 and PB3, with PB1 and PB2 creating an antiparallel  β and PB3 sitting perpendicularly to PB2. All substrate binding sites of the various esterases, hydrolases, and lyases are located on an outer cleft of the central parallel β-helix structure between protruding loops on the structure and PB1.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a>
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<h2 id="optimum-environment">Optimum environment</h2>
<p>As with all <a href="/facts/Enzymes/DSI1Fh7y">enzymes</a>, pectinases have an optimum temperature and <a href="/facts/PH/RnSv8D7y">pH</a> at which they are most active. For example, a commercial pectinase might typically be activated at 45 to 55 °C and work well at a pH of 3.0 to 6.5.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a>
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<h2 id="industrial-uses">Industrial uses</h2>
<p>Pectinase enzymes play various roles in both the fruit juice and wine industries. They are used for clarification in fruit juices and also speed up fruit juice extraction through enzymatic liquefaction of fruit pulp. In addition, pectinase enzymes aid in formation of pulpy products in the fruit juice industry. Pectinase enzymes are used for extracting juice from <a href="/facts/Pur%25C3%25A9e/a6E1xHAa">purée</a>. This is done when the enzyme pectinase breaks down the substrate pectin and the juice is extracted. The enzyme pectinase lowers the <a href="/facts/Activation_energy/GqkgPvo0">activation energy</a> needed for the juice to be produced and catalyzes the reaction.
</p><p>Pectinases are useful in the wine industry by extracting <a href="/facts/Anthocyanin/eUY12Frv">anthocyanin</a> from the fruit, effectively intensifying the wine coloring.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> Pectinase can also be used to extract juices from cell walls of plants cells.
</p><p>Pectinases are also used for <a href="/facts/Retting/A3Mm5u81">retting</a> in the textile industry.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> Addition of chelating agents or pretreatment of the plant material with acid enhance the effect of the enzyme.
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<h2 id="references">References</h2>

<ol>
<li id="fn:1"><p>Sakai T, Sakamoto T, Hallaert J, Vandamme EJ (1993). "Pectin, pectinase and protopectinase: production, properties, and applications". Advances in Applied Microbiology. 39: 213–94. doi:10.1016/s0065-2164(08)70597-5. PMID 8213306. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li>
<li id="fn:2"><p>Singh, Ram Sarup; Singh, Taranjeet; Pandey, Ashok (2019-01-01), Singh, Ram Sarup; Singhania, Reeta Rani; Pandey, Ashok; Larroche, Christian (eds.), "Chapter 1 - Microbial Enzymes—An Overview", Advances in Enzyme Technology, Biomass, Biofuels, Biochemicals, Elsevier, pp. 1–40, ISBN 978-0-444-64114-4, retrieved 2021-10-20 <a href="978-0-444-64114-4" target="_blank">978-0-444-64114-4</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li>
<li id="fn:3"><p>"Pectinase". Enzyme India. Archived from the original on 26 March 2010. Retrieved 26 March 2010. <a href="https://web.archive.org/web/20100326062407/http://www.enzymeindia.com:80/Enzymes-Pectinase.php" target="_blank">https://web.archive.org/web/20100326062407/http://www.enzymeindia.com:80/Enzymes-Pectinase.php</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li>
<li id="fn:4"><p>Melton, Laurence (2019). Encyclopedia of Food Chemistry (Volume 2 ed.). Elsevier. p. 271. <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li>
<li id="fn:5"><p>Saranaj, P; Naidu, M.A. (2014). "Microbial Pectinases: A Review". ResearchGate. <a href="https://www.researchgate.net/publication/261098549" target="_blank">https://www.researchgate.net/publication/261098549</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li>
<li id="fn:6"><p>Saranaj, P; Naidu, M.A. (2014). "Microbial Pectinases: A Review". ResearchGate. <a href="https://www.researchgate.net/publication/261098549" target="_blank">https://www.researchgate.net/publication/261098549</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li>
<li id="fn:7"><p>Sakai T, Sakamoto T, Hallaert J, Vandamme EJ (1993). "Pectin, pectinase and protopectinase: production, properties, and applications". Advances in Applied Microbiology. 39: 213–94. doi:10.1016/s0065-2164(08)70597-5. PMID 8213306. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li>
<li id="fn:8"><p>Saranaj, P; Naidu, M.A. (2014). "Microbial Pectinases: A Review". ResearchGate. <a href="https://www.researchgate.net/publication/261098549" target="_blank">https://www.researchgate.net/publication/261098549</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li>
<li id="fn:9"><p>"BRENDA - Information on EC 3.2.1.15 - endo-polygalacturonase". brenda-enzymes.org. Retrieved 2021-10-20. <a href="https://brenda-enzymes.org/enzyme.php?ecno=3.2.1.15" target="_blank">https://brenda-enzymes.org/enzyme.php?ecno=3.2.1.15</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li>
<li id="fn:10"><p>Gummadi, Sathyanarayana N.; Manoj, N.; Kumar, D. Sunil (2007), Polaina, Julio; MacCabe, Andrew P. (eds.), "Structural and Biochemical Properties of Pectinases", Industrial Enzymes: Structure, Function and Applications, Dordrecht: Springer Netherlands, pp. 99–115, doi:10.1007/1-4020-5377-0_7, ISBN 978-1-4020-5377-1, retrieved 2021-10-20 <a href="978-1-4020-5377-1" target="_blank">978-1-4020-5377-1</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li>
<li id="fn:11"><p>"Pectinase". Enzyme India. Archived from the original on 26 March 2010. Retrieved 26 March 2010. <a href="https://web.archive.org/web/20100326062407/http://www.enzymeindia.com:80/Enzymes-Pectinase.php" target="_blank">https://web.archive.org/web/20100326062407/http://www.enzymeindia.com:80/Enzymes-Pectinase.php</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li>
<li id="fn:12"><p>Saranaj, P; Naidu, M.A. (2014). "Microbial Pectinases: A Review". ResearchGate. <a href="https://www.researchgate.net/publication/261098549" target="_blank">https://www.researchgate.net/publication/261098549</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li>
<li id="fn:13"><p>Rebello, Sharrel; Anju, Mohandas; Aneesh, Embalil Mathachan; Sindhu, Raveendran; Binod, Parameswaran; Pandey, Ashok (13 July 2017). "Recent advancement sin the production and application of microbial pectinases: an overview" (PDF). Reviews in Environmental Science and Bio/Technology. 16 (3): 381–394. doi:10.1007/s11157-017-9437-y. S2CID 90607593. <a href="https://link.springer.com/content/pdf/10.1007/s11157-017-9437-y.pdf" target="_blank">https://link.springer.com/content/pdf/10.1007/s11157-017-9437-y.pdf</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li>
</ol>

Pectinase open-in-new

Pectinase