Unlocking green startup investments: How environmental policy pressures drive Venture Capital funding decisions

The urgency of addressing climate change has spotlighted the role of green startups. Independent (IVCs), Corporate (CVCs), and Governmental (GVCs) Venture Capitalists are key players in financing these startups. This study examines how public environmental policies influence the investment decisions of different VCs toward green startups, addressing a gap in understanding the interplay between VCs' behavior and policy frameworks. Drawing on Real Option, Open Innovation, Agency, and New Institutional theories and leveraging a panel dataset of 6754 VCs investments in 13,015 startups (2010–2019) from Crunchbase, Compustat, and OECD Environmental Policy Stringency data, our findings reveal that GVCs and CVCs have a positive propensity to invest in green startups, while IVCs have a negative one. Moreover, incentives do not reduce IVCs' investments while encouraging CVCs' funding in green startups. Conversely, constraints mitigate the risk perceived by IVCs, fostering their propensity to invest in green startups while discouraging CVCs. We contribute to the literature on the influence of environmental policies on investments by introducing a theory-driven classification of environmental policies and demonstrating that policy effectiveness varies across VC types due to their different investment logic. These insights guide policymakers in designing tailored incentives and constraints to mobilize private capital toward green startups

HOW DO ENVIRONMENTAL POLICY MECHANISMS INTERVENE IN THE IVCs AND CVCs DECISIONS TO INVEST IN SUSTAINABLE STARTUPS?

Sustainable startups have been recognized as crucial actors in fighting climate change and develop new technologies to reduce environmental harm (Bendig et al., 2022; Hegeman and Sørheim, 2021). Indeed, sustainable startups have critical capabilities and technical know-how to carry out the development of clean and green technologies to achieve sustainable change (Hockerts and Wüstenhagen, 2010). To survive and market such technologies sustainable startups need to overcome their unfavorable financial conditions by attracting external funding from Venture Capitalists (VCs), which have been largely recognized as the main catalyst for sustainable startups’ success (e.g., Wöhler and Haase, 2022). Specifically, sustainable startups as the opportunities to attract funding from different kinds of VCs, such as independent venture capitalists (IVCs) and corporate venture capitalists (CVCs) (e.g., Cumming et al., 2016; Bürer and Wüstenhagen, 2009; Polzin, 2017; Hegeman and Sørheim, 2021). Previous scholars have revealed that while CVCs are increasingly investing in sustainable startups, they represent a less attractive investment alternative than conventional ones for IVCs (Hegeman and Sørheim, 2021; Wöhler and Haase, 2022). Indeed, since IVCs usually aim to gain extraordinary and short-term return, the high technological risk and the very long development times characterizing green technologies may discourage them (Beise and Rennings, 2005). Moreover, IVCs may avoid investments in sustainable startups since the financial opportunities of green technologies cannot be totally captured due to their public nature (Cumming et al., 2016). Conversely, CVCs are strongly motivated to fund sustainable startups by the strategic value of the opportunities associated to clean and green technologies, which allow CVCs to improve their environmental performance and promote corporate greening in customers’ eyes for sustaining their competitive positions (Hegeman and Sørheim, 2021). All these things considered it is evident that , in accordance with their investment objectives, IVCs and CVCs have diverse investing inclinations toward sustainable startups. We reason that differences in the investment inclinations of IVCs and CVCs toward sustainable startups may also be explained by other exogenous factors such as national and international policies, which often focus on promoting sustainability. Current literature has already demonstrated that investments in sustainability can be stimulated by several environmental policy mechanisms such as feed-in tariffs, environmental taxes, emission trading schemes, emission limits and R&D subsidies (Bürer and Wüstenhagen, 2009; Polzin et al., 2017; Criscuolo and Menon, 2015; Bianchini and Croce, 2022). However, there is no evidence on how these policy mechanisms intervene in the inclinations of diverse VCs investors toward funding sustainable startups. Thus, this paper aims to better understand the role of national and international policies in the VCs financing by exploring how diverse environmental policy mechanisms intervene in the VCs investments inclinations toward sustainable startups, by discerning the effect on IVCs and CVCs

Linking Circular Business Models With Value Sources: A Cluster‐Based Literature Review

Circular Business Models (CBMs) are critical to advancing the Circular Economy (CE), receiving significant attention from policymakers and corporations alike. Despite this, the conceptual clarity of CBMs remains underdeveloped. This paper presents a systematic literature review of CBM, focusing on definitions, drivers, barriers, and value creation. We identify three primary clusters: CBM concept, CBM transformation, and CBM strategies. Key gaps in the literature are highlighted, with particular regard to market value creation, comprehensive business model framework, and firm maturity. To address these gaps, we propose a framework linking CBM strategies with value sources, offering a more cohesive understanding of circularity within business models. This framework aims to guide future research and practical implementation across various firm maturity stages

Nudging the Last Mile: Combining Behavioral Insights and Monetary Incentives for Sustainable Delivery Choices

Last mile delivery, the final leg of the supply chain to consumers, significantly impacts the en- vironment. The role of consumers’ behavior in this process, has been relatively overlooked and their willingness to find a trade-off between the benefits of home delivery and the impact on the environment has been neglected; behavioral logistics aims to optimize supply chain operations by understanding and influencing human behavior, enhancing efficiency and sustainability. Consumer behavior within the grocery sector is influenced by a myriad of factors and the rise of environ- mental awareness among consumers provides an opportunity to impact their preferences, steering them towards more sustainable last mile delivery options. The importance of home deliveries in the grocery sector has surged, especially post-pandemic; grocery stores adapt to this trend, focusing on efficient last mile delivery to meet changing consumer demands. By utilizing the experimental economics methodology tailored to the grocery sector, this research systematically examines the impact of financial incentives and nudges on last mile delivery choices. The controlled environment offers valuable insights into consumer responses to various incentive structures, helping to shape strategies that maximize both environmental benefits and economic sustainability. The findings underscore the interplay between environmental sustainability, consumer behavior, financial incen- tives, and nudges in the last mile delivery of groceries providing valuable insights for businesses, policymakers, and consumers in their collective endeavor to build a more sustainable and efficient last mile delivery system

High-throughput, quantitative analyses of genetic interactions in E. coli.

Large-scale genetic interaction studies provide the basis for defining gene function and pathway architecture. Recent advances in the ability to generate double mutants en masse in Saccharomyces cerevisiae have dramatically accelerated the acquisition of genetic interaction information and the biological inferences that follow. Here we describe a method based on F factor-driven conjugation, which allows for high-throughput generation of double mutants in Escherichia coli. This method, termed genetic interaction analysis technology for E. coli (GIANT-coli), permits us to systematically generate and array double-mutant cells on solid media in high-density arrays. We show that colony size provides a robust and quantitative output of cellular fitness and that GIANT-coli can recapitulate known synthetic interactions and identify previously unidentified negative (synthetic sickness or lethality) and positive (suppressive or epistatic) relationships. Finally, we describe a complementary strategy for genome-wide suppressor-mutant identification. Together, these methods permit rapid, large-scale genetic interaction studies in E. coli

The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity

The outer membrane (OM) of Gram-negative pathogenic bacteria is a key structure in host–pathogen interactions that contains a plethora of proteins, performing a range of functions including adhesion, nutrient uptake, export of effectors and interaction with innate and adaptive components of the immune system. In addition, the OM can exclude drugs and thus contribute to antimicrobial resistance. The OM of the food-borne pathogen Campylobacter jejuni contains porins, adhesins and other virulence factors that must be specifically localized to this membrane, but the protein sorting mechanisms involved are only partially understood. In particular, chaperones are required to ferry OM proteins across the periplasm after they emerge from the Sec translocation system. The SurA-related chaperone PEB4 (Cj0596) is the only protein with a proven role in OM biogenesis and integrity in C. jejuni. In this work, we have constructed a set of isogenic deletion mutants in genes encoding both known and predicted chaperones (cj0596, cj0694, cj1069, cj1228c, and cj1289) using NCTC 11168H as the parental strain. These mutants were characterized using a range of assays to determine effects on growth, agglutination, biofilm formation, membrane permeability and hydrophobicity. We focused on Cj1289 and Cj0694, which our previous work suggested possessed both chaperone and peptidyl-proyl cis/trans isomerase (PPIase) domains. Mutants in either cj1289 or cj0694 showed growth defects, increased motility, agglutination and biofilm formation and severe OM permeability defects as measured by a lysozyme accessibility assay, that were comparable to those exhibited by the isogenic peb4 mutant. 2D-gel comparisons showed a general decrease in OM proteins in these mutants. We heterologously overproduced and purified Cj0694 and obtained evidence that this protein was an active PPIase, as judged by its acceleration of the refolding rate of reduced and alkylated ribonuclease T1 and that it also possessed holdase-type chaperone activity. Cj0694 is most similar to the PpiD class of chaperones but is unusual in possessing PPIase activity. Taken together, our data show that in addition to PEB4, Cj1289 (SalC; SurA-like chaperone) and Cj0694 (PpiD) are also key proteins involved in OM biogenesis and integrity in C. jejuni

Factors Affecting the Folding of Pseudomonas aeruginosa OprF Porin into the One-Domain Open Conformer

Pseudomonas aeruginosa OprF is a largely monomeric outer membrane protein that allows the slow, nonspecific transmembrane diffusion of solutes. This protein folds into two different conformers, with the majority conformer folding into a two-domain conformation that has no porin activity and the minority conformer into a one-domain conformation with high porin activity and presumably consisting of a large β barrel. We examined the factors that control the divergent folding pathways of OprF. OprF contains four Cys residues in the linker region connecting the N-terminal β-barrel domain and the C-terminal globular domain in the majority conformer. Prevention of disulfide bond formation either by expression of OprF in an Escherichia coli dsbA strain grown with dithiothreitol or by replacement of all Cys residues with serine (CS OprF) increased the specific pore-forming activity of OprF significantly. Replacement of Phe160 with Ile at the end of the β-barrel termination signal as well as replacement of Lys164 in the linker region with Gly, Cys, or Glu increased porin activity 2-fold. Improving a potential β-barrel termination signal in the periplasmic domain by replacement of Asp211 with asparagine also increased porin activity. The porin activity could be improved about 5-fold by the combination of these replacements. OprF mutants with higher porin activity were shown to contain more one-domain conformers by surface labeling of the A312C residue in intact cells, as this residue is located in the periplasmic domain in the two-domain conformers. Finally, when the OprF protein was expressed in an E. coli strain lacking the periplasmic chaperone Skp, the CS OprF protein exhibited increased pore-forming activity

Periplasmic chaperone FkpA is essential for imported colicin M toxicity

Chaperones facilitate correct folding of newly synthesized proteins. We show here that the periplasmic FkpA chaperone is required for killing Escherichia coli by colicin M entering cells from the outside. Highly active colicin M preparations were inactive against fkpA mutant cells; 104-fold dilutions killed fkpA+ cells. Three previously isolated spontaneous mutants tolerant to colicin M carried a stop codon or an IS1 insertion in the peptidyl-prolyl-cis-trans-isomerase (PPIase) domain (C-domain) of FkpA, which resulted in deletion of the domain. A randomly generated mutant carried a G148D mutation in the C-domain. A temperature-sensitive mutant tolerant to colicin M carried a Y25N mutation in the FkpA N-domain. Mutants transformed with wild-type fkpA were colicin M-sensitive. Isolated FkpA-His reduced colicin M-His cleavage by proteinase K and renatured denatured colicin M-His in vitro; renaturation was prevented by the PPIase inhibitor FK506. In both assays, periplasmic SurA-His had no effect. No other tested periplasmic chaperone could activate colicin M. Among the tested colicins, only colicin M required FkpA for activity. Colicin M bound to cells via FhuA was inactivated by trypsin; unbound colicin M retained activity. We propose that colicin M unfolds during import across the outer membrane, FkpA specifically assists in folding colicin M into an active toxin in the periplasm and PPIase is essential for colicin M activity. Colicin M is a suitable tool for the isolation of FkpA mutants used to elucidate the functions of the FkpA N- and C-domains

Components of SurA Required for Outer Membrane Biogenesis in Uropathogenic Escherichia coli

Background: SurA is a periplasmic peptidyl-prolyl isomerase (PPIase) and chaperone of Escherichia coli and other Gramnegative bacteria. In contrast to other PPIases, SurA appears to have a distinct role in chaperoning newly synthesized porins destined for insertion into the outer membrane. Previous studies have indicated that the chaperone activity of SurA rests in its ‘‘core module’ ’ (the N- plus C-terminal domains), based on in vivo envelope phenotypes and in vitro binding and protection of non-native substrates. Methodology/Principal Findings: In this study, we determined the components of SurA required for chaperone activity using in vivo phenotypes relevant to disease causation by uropathogenic E. coli (UPEC), namely membrane resistance to permeation by antimicrobials and maturation of the type 1 pilus usher FimD. FimD is a SurA-dependent, integral outer membrane protein through which heteropolymeric type 1 pili, which confer bladder epithelial binding and invasion capacity upon uropathogenic E. coli, are assembled and extruded. Consistent with prior results, the in vivo chaperone activity of SurA in UPEC rested primarily in the core module. However, the PPIase domains I and II were not expendable for wild-type resistance to novobiocin in broth culture. Steady-state levels of FimD were substantially restored in the UPEC surA mutant complemented with the SurA N- plus C-terminal domains. The addition of PPIase domain I augmented FimD maturation into the outer membrane, consistent with a model in which domain I enhances stability of and/or substrat

Reversal of the ΔdegP Phenotypes by a Novel rpoE Allele of Escherichia coli

RseA sequesters RpoE (σE) to the inner membrane of Escherichia coli when envelope stress is low. Elevated envelope stress triggers RseA cleavage by the sequential action of two membrane proteases, DegS and RseP, releasing σE to activate an envelope stress reducing pathway. Revertants of a ΔdegP ΔbamB strain, which fails to grow at 37°C due to high envelope stress, harbored mutations in the rseA and rpoE genes. Null and missense rseA mutations constitutively hyper-activated the σE regulon and significantly reduced the major outer membrane protein (OMP) levels. In contrast, a novel rpoE allele, rpoE3, resulting from the partial duplication of the rpoE gene, increased σE levels greater than that seen in the rseA mutant background but did not reduce OMP levels. A σE-dependent RybB::LacZ construct showed only a weak activation of the σE pathway by rpoE3. Despite this, rpoE3 fully reversed the growth and envelope vesiculation phenotypes of ΔdegP. Interestingly, rpoE3 also brought down the modestly activated Cpx envelope stress pathway in the ΔdegP strain to the wild type level, showing the complementary nature of the σE and Cpx pathways. Through employing a labile mutant periplasmic protein, AcrAL222Q, it was determined that the rpoE3 mutation overcomes the ΔdegP phenotypes, in part, by activating a σE-dependent proteolytic pathway. Our data suggest that a reduction in the OMP levels is not intrinsic to the σE-mediated mechanism of lowering envelope stress. They also suggest that under extreme envelope stress, a tight homeostasis loop between RseA and σE may partly be responsible for cell death, and this loop can be broken by mutations that either lower RseA activity or increase σE levels