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		<title>BioCat Collective</title>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/coupling-enzyme-activity-to-host-survival-via-genetic-code-expansion-an-in-vivo-evolution-system-for-biocatalysts/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/coupling-enzyme-activity-to-host-survival-via-genetic-code-expansion-an-in-vivo-evolution-system-for-biocatalysts/]]></link>
			<title>Coupling Enzyme Activity to Host Survival via Genetic Code Expansion: An In Vivo Evolution System for Biocatalysts</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 06:05:50 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/inhibitors-enable-rapid-start-up-and-stable-operation-of-partial-nitrification-effects-mechanisms-and-challenges/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/inhibitors-enable-rapid-start-up-and-stable-operation-of-partial-nitrification-effects-mechanisms-and-challenges/]]></link>
			<title>Inhibitors enable rapid start-up and stable operation of partial nitrification: Effects, mechanisms and challenges</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 06:05:50 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/kinetic-and-molecular-insights-into-ion-specific-regulation-of-nattokinase-by-divalent-metal-ions/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/kinetic-and-molecular-insights-into-ion-specific-regulation-of-nattokinase-by-divalent-metal-ions/]]></link>
			<title>Kinetic and molecular insights into ion-specific regulation of nattokinase by divalent metal ions</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 06:05:47 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/continuous-gas-fermentation-for-acetate-production-at-pilot-scale-utilising-biogenic-co2-recovered-from-biogas-upgrading/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/continuous-gas-fermentation-for-acetate-production-at-pilot-scale-utilising-biogenic-co2-recovered-from-biogas-upgrading/]]></link>
			<title>Continuous gas fermentation for acetate production at pilot scale utilising biogenic CO2 recovered from biogas upgrading</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 06:05:47 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/living-spatially-organized-hybrid-condensates-for-efficient-light-driven-co2-to-chemical-conversion/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/living-spatially-organized-hybrid-condensates-for-efficient-light-driven-co2-to-chemical-conversion/]]></link>
			<title>Living Spatially Organized Hybrid Condensates for Efficient Light-Driven CO2-to-Chemical Conversion</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 00:06:33 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/molecular-diversity-generation-via-selective-enzymatic-c-cn-bond-scission/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/molecular-diversity-generation-via-selective-enzymatic-c-cn-bond-scission/]]></link>
			<title>Molecular Diversity Generation via Selective Enzymatic C-CN Bond Scission</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 00:06:33 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/structurally-characterized-haloacid-dehalogenase-4a-catalyzes-fluoroacetate-defluorination-and-provides-a-scaffold-for-exploring-organofluorine-c─f-bond-cleavage/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/structurally-characterized-haloacid-dehalogenase-4a-catalyzes-fluoroacetate-defluorination-and-provides-a-scaffold-for-exploring-organofluorine-c─f-bond-cleavage/]]></link>
			<title>Structurally Characterized Haloacid Dehalogenase 4A Catalyzes Fluoroacetate Defluorination and Provides a Scaffold for Exploring Organofluorine C─F Bond Cleavage</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 00:06:32 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/conserved-selectivity-patterns-in-pyran-synthases-revealed-by-studies-on-sorps8/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/conserved-selectivity-patterns-in-pyran-synthases-revealed-by-studies-on-sorps8/]]></link>
			<title>Conserved Selectivity Patterns in Pyran Synthases Revealed by Studies on SorPS8</title>
			<pubDate><![CDATA[Thu, 12 Nov 2026 00:06:32 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/nanocatalytic-anti-inflammatory-therapy-for-alleviating-rheumatoid-lesions-with-endothelial-cell-derived-hydrosilicene/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/nanocatalytic-anti-inflammatory-therapy-for-alleviating-rheumatoid-lesions-with-endothelial-cell-derived-hydrosilicene/]]></link>
			<title>Nanocatalytic anti-inflammatory therapy for alleviating rheumatoid lesions with endothelial cell-derived hydrosilicene</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 18:04:29 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/enhancing-ω-transaminase-catalysis-of-bulky-substrates-guided-by-binding-mechanism/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/enhancing-ω-transaminase-catalysis-of-bulky-substrates-guided-by-binding-mechanism/]]></link>
			<title>Enhancing ω-transaminase catalysis of bulky substrates guided by binding mechanism</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 18:04:28 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/biodegradation-mechanisms-of-pbde-209-enzymatic-microbial-and-omics-driven-insights/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/biodegradation-mechanisms-of-pbde-209-enzymatic-microbial-and-omics-driven-insights/]]></link>
			<title>Biodegradation mechanisms of PBDE - 209: enzymatic, microbial, and omics-driven insights</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 18:04:28 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/discovery-of-novel-endolytic-hyaluronate-lyases-belonging-to-a-new-subfamily-of-gh56-and-enhancement-of-catalytic-activity-through-catalytic-cleft-engineering/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/discovery-of-novel-endolytic-hyaluronate-lyases-belonging-to-a-new-subfamily-of-gh56-and-enhancement-of-catalytic-activity-through-catalytic-cleft-engineering/]]></link>
			<title>Discovery of Novel Endolytic Hyaluronate Lyases Belonging to a New Subfamily of GH56 and Enhancement of Catalytic Activity through Catalytic Cleft Engineering</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 18:04:28 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/recent-advances-in-the-synthesis-of-imidazo21-aisoquinolines-and-their-core-embedded-heterocycles/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/recent-advances-in-the-synthesis-of-imidazo21-aisoquinolines-and-their-core-embedded-heterocycles/]]></link>
			<title>Recent advances in the synthesis of imidazo[2,1-&lt;em&gt;a&lt;/em&gt;]isoquinolines and their core-embedded heterocycles</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 18:04:28 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/protein-language-model-assisted-engineering-of-a-high-performance-polyethylene-terephthalate-hydrolase-for-enhanced-biorecycling/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/protein-language-model-assisted-engineering-of-a-high-performance-polyethylene-terephthalate-hydrolase-for-enhanced-biorecycling/]]></link>
			<title>Protein language model-assisted engineering of a high-performance polyethylene terephthalate hydrolase for enhanced biorecycling</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 06:05:15 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/high-level-de-novo-biosynthesis-of-pyridoxal-5-phosphate-in-bacillus-licheniformis-by-systems-engineering/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/high-level-de-novo-biosynthesis-of-pyridoxal-5-phosphate-in-bacillus-licheniformis-by-systems-engineering/]]></link>
			<title>High-level de novo biosynthesis of pyridoxal 5&#8242;-phosphate in Bacillus licheniformis by systems engineering</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 06:05:15 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/reprogramming-flavonoid-glycosylation-by-bridging-advanced-biocatalysis-and-systems-synthetic-biology/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/reprogramming-flavonoid-glycosylation-by-bridging-advanced-biocatalysis-and-systems-synthetic-biology/]]></link>
			<title>Reprogramming flavonoid glycosylation by bridging advanced biocatalysis and systems synthetic biology</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 06:05:15 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/a-scalable-whole-cell-biocatalytic-process-for-food-compatible-production-of-resolvin-d5-using-the-edible-mushroom-pleurotus-ostreatus/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/a-scalable-whole-cell-biocatalytic-process-for-food-compatible-production-of-resolvin-d5-using-the-edible-mushroom-pleurotus-ostreatus/]]></link>
			<title>A scalable whole-cell biocatalytic process for food-compatible production of resolvin D5 using the edible mushroom Pleurotus ostreatus</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 06:05:15 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/characterization-of-monoterpene-and-sesquiterpene-synthases-from-nardostachys-jatamansi/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/characterization-of-monoterpene-and-sesquiterpene-synthases-from-nardostachys-jatamansi/]]></link>
			<title>Characterization of monoterpene and sesquiterpene synthases from &lt;em&gt;Nardostachys jatamansi&lt;/em&gt;</title>
			<pubDate><![CDATA[Wed, 11 Nov 2026 00:02:17 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/cu-n4-single-atom-nanozyme-with-multi-enzyme-mimetic-activities-combined-with-in2o3-bi24o31br10-heterojunction-toward-sensitive-triple-mode-detection-and-photocatalytic-inactivation-of-vi/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/cu-n4-single-atom-nanozyme-with-multi-enzyme-mimetic-activities-combined-with-in2o3-bi24o31br10-heterojunction-toward-sensitive-triple-mode-detection-and-photocatalytic-inactivation-of-vi/]]></link>
			<title>Cu-N(4) Single-Atom Nanozyme with Multi-Enzyme Mimetic Activities Combined with In(2)O(3)/Bi(24)O(31)Br(10) Heterojunction: Toward Sensitive Triple-Mode Detection and Photocatalytic Inactivation of Vibrio Alginolyticus</title>
			<pubDate><![CDATA[Tue, 10 Nov 2026 18:02:35 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/enzyme-systems-immobilized-using-metal-organic-frameworks-as-plant-cell-mimics-for-converting-co2-into-organic-matter-feasibility-design-principles-and-translational-challenges/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/enzyme-systems-immobilized-using-metal-organic-frameworks-as-plant-cell-mimics-for-converting-co2-into-organic-matter-feasibility-design-principles-and-translational-challenges/]]></link>
			<title>Enzyme systems immobilized using metal-organic frameworks as plant cell mimics for converting CO2 into organic matter: Feasibility, design principles and translational challenges</title>
			<pubDate><![CDATA[Tue, 10 Nov 2026 06:03:31 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/ftmox1-catalyzed-diverse-csp3-h-oxyfunctionalization-enables-versatile-late-stage-diversification-of-phenethylamines-and-tetrahydroisoquinolines/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/ftmox1-catalyzed-diverse-csp3-h-oxyfunctionalization-enables-versatile-late-stage-diversification-of-phenethylamines-and-tetrahydroisoquinolines/]]></link>
			<title>FtmOx1-catalyzed diverse C(sp3)-H oxyfunctionalization enables versatile late-stage diversification of phenethylamines and tetrahydroisoquinolines</title>
			<pubDate><![CDATA[Mon, 09 Nov 2026 18:05:45 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/evolution-inspired-multi-objective-bayesian-optimization-for-protein-engineering/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/evolution-inspired-multi-objective-bayesian-optimization-for-protein-engineering/]]></link>
			<title>Evolution-Inspired Multi-Objective Bayesian Optimization for Protein Engineering</title>
			<pubDate><![CDATA[Mon, 09 Nov 2026 00:00:24 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/de-novo-design-of-a-vanadium-haloperoxidase/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/de-novo-design-of-a-vanadium-haloperoxidase/]]></link>
			<title>De novo Design of a Vanadium Haloperoxidase</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 23:04:14 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/eight-electron-reduction-of-co2-to-ch4-by-a-bioinspired-mo-fe-s-cubane-catalyst/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/eight-electron-reduction-of-co2-to-ch4-by-a-bioinspired-mo-fe-s-cubane-catalyst/]]></link>
			<title>Eight-Electron Reduction of CO2 to CH4 by a Bioinspired Mo-Fe-S Cubane Catalyst</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 18:10:29 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/protein-scaffolds-modulate-the-electronic-structure-of-a-common-ketyl-radical-intermediate-in-thiamine-pyrophosphate-dependent-radical-biocatalysis-insights-from-epr-and-endor-spectroscopy/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/protein-scaffolds-modulate-the-electronic-structure-of-a-common-ketyl-radical-intermediate-in-thiamine-pyrophosphate-dependent-radical-biocatalysis-insights-from-epr-and-endor-spectroscopy/]]></link>
			<title>Protein Scaffolds Modulate the Electronic Structure of a Common Ketyl Radical Intermediate in Thiamine Pyrophosphate-Dependent Radical Biocatalysis: Insights from EPR and ENDOR Spectroscopy</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 18:10:28 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/diterpene-cyclases-can-transform-unnatural-cis-allylic-pyrophosphate-substrates-into-inaccessible-scaffolds/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/diterpene-cyclases-can-transform-unnatural-cis-allylic-pyrophosphate-substrates-into-inaccessible-scaffolds/]]></link>
			<title>Diterpene Cyclases Can Transform Unnatural Cis-allylic Pyrophosphate Substrates Into Inaccessible Scaffolds</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 06:00:10 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/refactoring-pikromycin-synthase-for-the-modular-biosynthesis-of-macrolide-antibiotics-in-e-coli/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/refactoring-pikromycin-synthase-for-the-modular-biosynthesis-of-macrolide-antibiotics-in-e-coli/]]></link>
			<title>Refactoring pikromycin synthase for the modular biosynthesis of macrolide antibiotics in &lt;em&gt;E. coli&lt;/em&gt;</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 06:00:10 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/sequential-regulation-of-dual-catalytic-modules-for-the-directed-biosynthesis-of-25-furandicarboxylic-acid-in-escherichia-coli/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/sequential-regulation-of-dual-catalytic-modules-for-the-directed-biosynthesis-of-25-furandicarboxylic-acid-in-escherichia-coli/]]></link>
			<title>Sequential regulation of dual catalytic modules for the directed biosynthesis of 2,5-furandicarboxylic acid in Escherichia coli</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 06:00:10 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/revisiting-carbonyl-reductase-stereocontrol-a-third-pocket-accommodates-the-e-ring-in-podophyllotoxone-type-ketone-reduction/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/revisiting-carbonyl-reductase-stereocontrol-a-third-pocket-accommodates-the-e-ring-in-podophyllotoxone-type-ketone-reduction/]]></link>
			<title>Revisiting Carbonyl Reductase Stereocontrol: A Third Pocket Accommodates the E Ring in Podophyllotoxone-Type Ketone Reduction</title>
			<pubDate><![CDATA[Sun, 08 Nov 2026 06:00:09 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/domain-specific-control-of-silica-aggregation-by-peptides-from-sorghum-siliplant1/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/domain-specific-control-of-silica-aggregation-by-peptides-from-sorghum-siliplant1/]]></link>
			<title>Domain-specific control of silica aggregation by peptides from sorghum Siliplant1</title>
			<pubDate><![CDATA[Sat, 07 Nov 2026 06:05:49 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/proximity-labeling-an-empowering-tool-for-deciphering-molecular-mechanisms/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/proximity-labeling-an-empowering-tool-for-deciphering-molecular-mechanisms/]]></link>
			<title>Proximity Labeling: An Empowering Tool for Deciphering Molecular Mechanisms</title>
			<pubDate><![CDATA[Sat, 07 Nov 2026 06:05:47 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/from-prediction-to-creation-how-ai-driven-design-is-reshaping-microbial-biocatalysis/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/from-prediction-to-creation-how-ai-driven-design-is-reshaping-microbial-biocatalysis/]]></link>
			<title>From prediction to creation: How AI-driven design is reshaping microbial biocatalysis</title>
			<pubDate><![CDATA[Sat, 07 Nov 2026 06:05:45 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/quef-nitrile-reductases-catalytic-mechanism-and-advances-in-biocatalyst-development/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/quef-nitrile-reductases-catalytic-mechanism-and-advances-in-biocatalyst-development/]]></link>
			<title>QueF nitrile reductases: Catalytic mechanism and advances in biocatalyst development</title>
			<pubDate><![CDATA[Fri, 06 Nov 2026 18:05:43 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/helixwings-enables-ai-driven-enzyme-engineering-for-biomimetic-cofactor-utilization/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/helixwings-enables-ai-driven-enzyme-engineering-for-biomimetic-cofactor-utilization/]]></link>
			<title>HelixWings enables AI-driven enzyme engineering for biomimetic cofactor utilization</title>
			<pubDate><![CDATA[Fri, 06 Nov 2026 18:05:43 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/expanding-the-galactose-oxidase-substrate-repertoire-via-a-multi-modal-computational-strategy/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/expanding-the-galactose-oxidase-substrate-repertoire-via-a-multi-modal-computational-strategy/]]></link>
			<title>Expanding the galactose oxidase substrate repertoire via a multi-modal computational strategy</title>
			<pubDate><![CDATA[Fri, 06 Nov 2026 18:05:43 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/β-glcy-treatment-alters-transcriptome-dynamics-and-auxin-distribution-during-microspore-embryogenesis-in-brassica-napus/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/β-glcy-treatment-alters-transcriptome-dynamics-and-auxin-distribution-during-microspore-embryogenesis-in-brassica-napus/]]></link>
			<title>β-GlcY treatment alters transcriptome dynamics and auxin distribution during microspore embryogenesis in Brassica napus</title>
			<pubDate><![CDATA[Fri, 06 Nov 2026 18:05:43 +0000]]></pubDate>
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			<guid><![CDATA[https://biocatcollective.emorychem.science/directed-evolution-of-artificial-enzyme-with-a-catalytic-noncanonical-amino-acid-for-asymmetric-friedel-crafts-alkylation-of-cyclic-enones-with-indoles/]]></guid>
			<link><![CDATA[https://biocatcollective.emorychem.science/directed-evolution-of-artificial-enzyme-with-a-catalytic-noncanonical-amino-acid-for-asymmetric-friedel-crafts-alkylation-of-cyclic-enones-with-indoles/]]></link>
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