Current and future polyalphaolefins

Blackwell, John; Bullen, J. V.; Shubkin, Ronald L.

doi:10.1002/jsl.3000070104

Cited by 10 publications

(4 citation statements)

References 5 publications

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“… , Since fatty acids are naturally abundant, their conversion into terminal olefins has attracted enormous scientific interest. Terminal olefins are also extensively used in various industries, such as polymer, lubricant, and detergent. − …”

Section: Intoductionmentioning

confidence: 99%

Unraveling the Conversion of Fatty Acids into Terminal Alkenes by an Integral Membrane Enzyme, UndB

Iqbal,

Murugan,

Rajendran

et al. 2023

ACS Catal.

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Biosynthetically produced 1-alkenes hold immense value as green alternatives to fossil fuels and find widespread applications in the polymer, lubricant, and detergent industries. UndB is the only known membrane enzyme capable of converting fatty acids into 1-alkenes with unprecedented in vivo titers. However, despite diverse applications, UndB has remained poorly understood since its discovery nearly a decade ago. We present here insights into the molecular basis of UndB catalysis and the mechanism of the UndB reaction at the membrane interface. We unravel UndB as a diiron-enzyme that utilizes a conserved histidine cluster at the active site. We decipher the dependency of UndB activity on molecular oxygen and electrons and identify the most efficient redox partners of UndB. We elucidate the catalytic intricacies of UndB and establish it as the most efficient decarboxylase in producing industrially valuable medium-chain 1-alkenes. We further identify CO2 as the C1-derived coproduct of the UndB-catalyzed reaction and provide compelling evidence supporting the hydrogen atom transfer mechanism of UndB. These results now place our understanding of UndB on a molecular level, paving the way for its application for sustainable 1-alkene production.

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Section: Intoductionmentioning

confidence: 99%

Unraveling the Conversion of Fatty Acids into Terminal Alkenes by an Integral Membrane Enzyme, UndB

Iqbal,

Murugan,

Rajendran

et al. 2023

ACS Catal.

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“…The corresponding terminal olefins are excellent fuel candidates and exhibit remarkable versatility owing to the presence of the olefin moiety, allowing facile derivatization and leading to utility in many value‐added products (Figure 1b). Medium to long‐chain olefins, particularly, find widespread application as key precursors for manufacturing detergents, polymers, lubricants, pesticides, cosmetics, and other industrial additives (Benda et al, 1996; Blackwell et al, 1990; Ray et al, 2012; Yu et al, 2022). Moreover, medium‐chain olefins can integrate with the existing transportation infrastructure, offering superior properties such as higher energy content than short‐chain olefins, lower freezing points than longer olefins, and facile product recovery due to their immiscibility in water (Liao et al, 2016; Peralta‐Yahya et al, 2012; Zhou et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Functional production and biochemical investigation of an integral membrane enzyme for olefin biosynthesis

Murugan,

Iqbal,

Das

2024

Protein Science

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Integral membrane enzymes play essential roles in a plethora of biochemical processes. The fatty acid desaturases (FADS)‐like superfamily is an important group of integral membrane enzymes that catalyze a wide array of reactions, including hydroxylation, desaturation, and cyclization; however, due to the membrane‐bound nature, the majority of these enzymes have remained poorly understood. UndB is a member of the FADS‐like superfamily, which catalyzes fatty acid decarboxylation, a chemically challenging reaction at the membrane interface. UndB reaction produces terminal olefins that are prominent biofuel candidates and building blocks of polymers with widespread industrial applications. Despite the great importance of UndB for several biotechnological applications, the enzyme has eluded comprehensive investigation. Here, we report details of the expression, solubilization, and purification of several constructs of UndB to achieve the optimally functional enzyme. We gained important insights into the biochemical, biophysical, and catalytic properties of UndB, including the thermal stability and factors influencing the enzyme activity. Additionally, we established the ability and kinetics of UndB to produce dienes by performing di‐decarboxylation of diacids. We found that the reaction proceeds by forming a mono‐carboxylic acid intermediate. Our findings shed light on the unexplored biochemical properties of the UndB and extend opportunities for its rigorous mechanistic and structural characterization.This article is protected by copyright. All rights reserved.

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“…Notably, the medium-chain 1-alkenes are promising biofuel candidates because of their exceptional properties, including low freezing point, high energy content, recovery convenience due to their insolubility in water, and compatibility with current engine systems and transportation infrastructures (5). 1-Alkenes are also heavily used as commodity chemicals in various industries as precursors of detergents, polymers, and lubricants (6)(7)(8)(9)(10), making them attractive molecules to biosynthesize. A feasible route to 1-alkene biosynthesis is the enzymatic one-step decarboxylation of naturally abundant free fatty acids by fatty acid decarboxylases (11,12).…”

Section: Introductionmentioning

confidence: 99%

A chimeric membrane enzyme and an engineered whole-cell biocatalyst for efficient 1-alkene production

Iqbal,

Murugan,

Das

2024

Sci. Adv.

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Bioproduction of 1-alkenes from naturally abundant free fatty acids offers a promising avenue toward the next generation of hydrocarbon-based biofuels and green commodity chemicals. UndB is the only known membrane-bound 1-alkene–producing enzyme, with great potential for 1-alkene bioproduction, but the enzyme exhibits limited turnovers, thus restricting its widespread usage. Here, we explore the molecular basis of the limitation of UndB activity and substantially improve its catalytic power. We establish that the enzyme undergoes peroxide-mediated rapid inactivation during catalysis. To counteract this inactivation, we engineered a chimeric membrane enzyme by conjugating UndB with catalase that protected UndB against peroxide and enhanced its number of turnovers tremendously. Notably, our chimeric enzyme is the only example of a membrane enzyme successfully engineered with catalase. We subsequently constructed a whole-cell biocatalytic system and achieved remarkable efficiencies (up to 95%) in the biotransformation of a wide range of fatty acids (both aliphatic and aromatic) into corresponding 1-alkenes with numerous biotechnological applications.

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Current and future polyalphaolefins

Cited by 10 publications

References 5 publications

Unraveling the Conversion of Fatty Acids into Terminal Alkenes by an Integral Membrane Enzyme, UndB

Unraveling the Conversion of Fatty Acids into Terminal Alkenes by an Integral Membrane Enzyme, UndB

Functional production and biochemical investigation of an integral membrane enzyme for olefin biosynthesis

A chimeric membrane enzyme and an engineered whole-cell biocatalyst for efficient 1-alkene production

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