Ginkgo Enzyme Solutions的封面图片
Ginkgo Enzyme Solutions

Ginkgo Enzyme Solutions

生物技术研究

Boston，Massachusetts 566 位关注者

Custom R&D services, high-performance enzyme panels, & licensable assets

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关于我们

We deliver high-performance enzymes to our clients. We offer custom R&D services, ready-to-screen Enzyme Panels, production strain engineering, and manufacturing process optimization. ????’???? ???????????????????????? ?????????????????? ???????????????? ???? ???????????? ??????????????????, ???????????????????? ?????? ??????????????????: ? Biocatalysts enabling novel reactions ? Optimized catalytic functions beyond what’s achievable with directed evolution and in fewer iterations using sophisticated ML approaches ? Improved production economics through increased expression titers and enhanced specific activities ?????????? ?????????? ?????? ?????? ?????? We use AI/ML-powered design, physics-based modeling, directed evolution, mining of natural diversity, and good old-fashioned biochemistry: our tech stack & expertise is deep. Our proprietary language models and automated computational platforms integrate the latest AI, simulation, and open-source tools. But we don’t use AI just for the sake of it. If another approach works better, we use it. ???????????? ?????? ???????????????????????????? With one of the largest protein databases and state-of-the-art screening facilities, we execute research programs at the scale needed to advance your technology. ???????????????? ???????? ???? ???????? ???????? ???? ?? Custom research services for enzyme discovery, optimization, and production ?? Licensable advanced enzymes, including ready-to-screen Enzyme Panels ?? Data generation services, ideal for training your own AI models Our experience spans pharma biocatalysis, molecular diagnostics and sequencing, and industrial green chemistry.

网站
https://biopharma.ginkgo.bio/
所属行业
生物技术研究
规模
501-1,000 人
总部
Boston，Massachusetts
创立
2009
领域
Enzyme Discovery、Enzyme Engineering、Protein Discovery、Strain Engineering、High-Throughput Screening和AI

动态

  • 查看Ginkgo Enzyme Solutions的组织主页
    Ginkgo Enzyme Solutions

    566 位关注者

    Introducing Ginkgo’s Enzyme Panels – the Next Generation in Biocatalyst Discovery ?? ????’?? ???????? ???? ?????????????? ???? ???????? ??????????????. Today, we are thrilled to announce the launch of three new Ready-Made Enzyme Panels, including novel oxidative transformations and emerging classes of interest. ???????????? ???????????? ???????????? ?? Unspecific Peroxygenases (UPOs) ?? 2ODD Chlorinases? ?? Lipases ?? Imine Reductases (IREDs) ?? 2ODD Hydroxylases ?? Custom Panels In addition, we provide custom enzyme services. Leveraging a 2.9B membered proprietary protein database and a powerful discovery platform, we source novel enzymes tailored to your needs. Let us design and build you a ???????????? ?????????? of enzymes.? ???????????????? ???? ?????? ?????????????? ???????????????? Prozomix Limited offers industry-leading CDMO services. Each panel is delivered as a 96-well plate(s) containing approximately 1 mg/well of lyophilized E. coli cell-free extracts, ready for immediate screening in your laboratory. Ready to try them out? ?? Schedule a 30-min call today → email us at [email protected] https://lnkd.in/gfMaSZcs #Biocatalysis #EnzymeEngineering #GinkgoEnzymeSolutions #EnzymePanels #APIManufacturing #GreenChemistry

  • The Ginkgo Enzyme Solutions team is onsite at #AGBT, soaking in the latest developments and big ideas shaping the future - and the Marco Island Breeze! ?? With one more day to go, there’s still time to connect! ?? Have a tough enzyme challenge? Let’s talk! Message Cindy Chang, Monica McNerney, or Jack Cavanaugh to set up a meeting before the conference wraps. #AGBT #GinkgoEnzymeSolutions #EnzymeEngineering #Biotech #SynBio

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  • 查看Ginkgo Enzyme Solutions的组织主页
    Ginkgo Enzyme Solutions

    566 位关注者

    We enjoyed this paper from Yan et al. (link in comment) which describes engineered variants of a promiscuous fungal prenyltransferase. The goal was to attach C5-C15 isoprenyl groups to olivetolic acid. With some optimization, the team demonstrated selective production of a previously undescribed compound – which turned out to have anti-inflammatory and antibacterial properties. Biochemists know well the challenges of efficiently exploring the vast combinatorial space in natural products! Many variables impact adduct synthesis and selective transfer to the core. At Ginkgo, we do a lot of enzyme engineering to enable natural product synthesis (both chemo-enzymatic and fermentation approaches). Engineering key pathway enzymes like prenyltransferases can open up new possibilities on both ends of your pharma pipeline: Discovery & Manufacturing. We have the infrastructure to help you navigate a space like this, including a prevalidated library of prenyltransferases to decorate core structures of interest in your R&D.

  • As researchers set out to engineer an enzyme, we naturally think first about its core target activity. But environment matters too: a viable biocatalyst needs high activity under relevant process conditions. Huang et al. (link in comment) combined structural analysis of the active site and evolutionary sequence analysis of the enzyme family to engineer α‐galactosidase for both higher catalytic activity and thermostability at 65 °C. They split their engineering into separate campaigns for activity and thermostability, and avoided mutations near the active site for the thermostability campaign to give the individual mutations the best chance of stacking into a single optimized variant at the end. We love this combination of design approaches to deliver an enzyme optimzed for multiple parameters that matter in application.

  • This has been a great week for protein engineering news! The latest excitement comes from today’s announcement from Roche on their "Sequencing By Expansion" technology, which relies on a highly engineered polymerase. We’re scurrying to read Keith Robison’s Omics! Omics! blog following the live webcast by Roche. Once you see the diagram of these massive, ~20kDa modified dNTPs, it’s easy to imagine that ???????? engineering tools went into developing a polymerase that could reliably incorporate those nucleotides (we’ll leave it to Keith and others to explain why this is a valuable innovation for sequencing). Indeed, the Roche team describes an “Xp synthase” with >10% of residues mutated from a unique translesion polymerase backbone. This looks like a story of iterations of thoughtful engineering exploring substantial diversity and rational hypotheses. This will surely be the talk of AGBT next week! We’re looking forward to talking about polymerase engineering among many other protein engineering topics key to pushing forward impactful sequencing technologies. AGBT - Advances in Genome Biology and Technology

  • Our team will be at AGBT next week! Looking forward to connecting in-person with collaborators and the broader genomics community. Who else will be there? ?? Connect with Cindy Chang Monica McNerney or Jack Cavanaugh and we’ll find time to chat

    查看Cindy Chang的档案
    Cindy Chang

    Sr Director Of Business Development at Ginkgo Bioworks, Inc.

    Hi LinkedIn Community! I will be at the AGBT conference on Marco Island next week. Please reach out if you will be there too and want to connect! Monica McNerney Jack Cavanaugh

  • Nice paper from the Max Planck Institute describing an engineered enzyme to enable a new metabolic pathway for CO? fixation! The team applied targeted mutations and adaptive evolution to develop a B??-dependent mutase that takes a 9-reaction CO? assimilation pathway down to 6 reactions. Adaptive evolution is a great way to explore a lot of genetic diversity. But it requires the phenotype of interest to be coupled to the cell’s growth, whereas most engineered pathways typically divert resources ???????? from growth. In this case, the team creatively engineered a growth-coupled selection strain (β-alanine auxotroph), enabling them to screen thousands of variants generated with random mutagenesis. Big picture: shorter pathways mean fewer catalysts and variables to optimize, typically reducing the risk to successful scale-up

    查看Helena Schulz-Mirbach的档案
    Helena Schulz-Mirbach

    Metabolic Engineer for a better future !

    Lets talk about #acetyl-CoA! As central molecule in C1 metabolism, the efficiency of its assimilation determines yields. Read below how we harnessed a novel enzymatic activity to design the shortest aerotolerant route to make pyruvate from acetyl-CoA while fixing #CO2! https://lnkd.in/eyDie7ud Despite its prevalence in #C1metabolism, the aerobic formation of gluconeogenic C3 compounds from acetyl-CoA has a pitfall: available routes either waste precious #carbon or are resource intensive. To overcome this limitation, we add a novel design to the pool: the Lcm module! We identified the lactyl-CoA mutase reaction as #newtonature enzyme activity and used it to build the shortest oxygen tolerant route to condense CO2 with acetyl-CoA and make the C3 intermediate pyruvate from it. For this, we repurposed a 2-HIB-CoA mutase to interconvert 3-HP-CoA and lactyl-CoA (Lcm reaction). After characterizing the novel activity in vitro & showing its functionality within our acetyl-CoA assimilation route, we set out to generate better enzyme variants. Indeed, the wild type Lcm activity was very slow (0.03 s-1) – but sufficed to support minute metabolic fluxes in vivo required for growth of a β-alanine #auxotrophic strain. This #growth dependency combined with the eMutaT7 system for in vivo #mutagenesis and selection for improved activity yielded three Lcm variants with 5-10 fold efficiency improvements! The mutations obtained in this evolution weren't targets we would have chosen for rational enzyme design – there is lots more for us to learn in the future. Hopefully, the Lcm lays a foundation to the success of new metabolism (for example CO2 fixation cycles!). This work had many contributors through the years – many thanks to all of them, and especially my wonderful co-first authors and amazing collaborators Philipp Wichmann and Ari Satanowski , and of course Tobias Erb .

  • We're excited to see this leap forward in halogenase biocatalysis published by the Tang group at UCLA. Kicking off the year strong for green chemistry! The researchers discovered what appears to be the **?????????? ?????? ???????????????????? ?????????? ???? ???? ?????????? ???? ??????????** In addition to C(sp3)–H chlorination, bromination and azidation, the unique copper center of this halogenase enables iodination and thiocyanation for the first time. You can do a lot of powerful chemistry after performing these types of selective functionalizations. If you’re interested in exploring this new class of halogenases, let’s discuss. https://lnkd.in/eD2tDhBT #biocatalysis #biopharma #GreenChemistry

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