Utilization of discard bovine bone as a support for immobilization of recombinant <i>Rhizopus oryzae</i> lipase expressed in <i>Pichia pastoris</i>

Clementz, Adriana Laura; Peso, Gonzalo Del; Canet, Albert; Yori, Juan Carlos; Valero, Francisco

doi:10.1002/btpr.2321

Cited by 4 publications

(4 citation statements)

References 36 publications

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“…Recently, 1,3‐specific immobilized lipases from Rhizomucor miehei (Lipozyme) and R. delemar (PP‐RhDL) were used in acidolysis of walnut oil with caprylic acid to synthesize long‐chain fatty acids . Also 1,3‐specific immobilized R. oryzae lipase expressed in Pichia pastoris was used for biodiesel production …”

Section: Lipase Structure and Classificationmentioning

confidence: 99%

“…In another study, an improved biocatalyst T. lanuginosus DSM 10635 lipase was engineered to improve its activity by using site‐saturation mutagenesis and high‐throughput screening techniques and effectively used in biosynthesis of chiral intermediate of Pregabalin . The study reported by Clementz et al, includes immobilization of recombinant R. oryzae lipase on bovine bone support which has shown high porosity, large surface area, and suitable porous structure, thereby resulting in improved biocatalytic activity of lipase. Further, two novel mutants of a psychrophilic lipase isolated from an arctic bacterium, B. pumilus were rationally designed based on the 3D‐structure model and resulted in significant improvement in their activities as compared with that of the wild type .…”

Section: Major Challenges With Respect To Industrial Implementationmentioning

confidence: 99%

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Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

273

148

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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Section: Lipase Structure and Classificationmentioning

confidence: 99%

Section: Major Challenges With Respect To Industrial Implementationmentioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

273

148

View full text Add to dashboard Cite

show abstract

“…Lipase is a class of enzymes with wide applications in industry . Lipase catalyzes various reactions such as hydrolysis, , esterification, , and transesterification. , Central to lipase activity is interfacial activation, which enhances activity upon adsorption on the interface between water and lipids. Candida antarctica lipase B (CALB) is one of the most widely used lipases in industry and academia and is utilized in various applications such as biodiesel production , and chemical synthesis. , …”

Section: Introductionmentioning

confidence: 99%

Energetic and Kinetic Origins of CALB Interfacial Activation Revealed by PaCS-MD/MSM

Wijaya,

Kitao

2023

J. Phys. Chem. B

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The conformational dynamics of Candida antarctica lipase B (CALB) was investigated by molecular dynamics (MD) simulation, parallel cascade selection MD (PaCS-MD), and the Markov state model (MSM) and mainly focused on the lid-opening motion closely related to substrate binding. All-atom MD simulation of CALB was conducted in water and on the interface of water and tricaprylin. CALB initially situated in water and separated by layers of water from the interface is spontaneously adsorbed onto the tricaprylin surface during MD simulation. The opening and closing motions of the lid are simulated by PaCS-MD, and subsequent MSM analysis provided the free-energy landscape and time scale of the conformational transitions among the closed, semiopen, and open states. The closed state is the most stable in the water system, but the stable conformation in the interface system shifts to the semiopen state. These effects could explain the energetics and kinetics origin of the previously reported interfacial activation of CALB. These findings could help expand the application of CALB toward a wide variety of substrates.

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“…Lipase is a class of enzymes with wide applications in industry 1 . Lipase catalyzes various reactions such as hydrolysis 2,3 , esterification 4,5 , and transesterification 6,7 . Central to lipase activity is interfacial activation 8 , which enhances activity upon adsorption on the interface between water and lipids.…”

Section: Introductionmentioning

confidence: 99%

Energetic and Kinetic Origin of CALB Interfacial Activation Revealed by PaCS-MD/MSM

Wijaya

Kitao

2023

Preprint

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Conformational dynamics of Candida antarctica Lipase B (CALB) was investigated by molecular dynamics (MD) simulation, parallel cascade selection MD (PaCS-MD), the Markov state model (MSM), and mainly focused on the lid-opening motion closely related to substrate binding. All-atom MD simulation of CALB was conducted in water and that around the interface constructed by water and tricaprylin. CALB initially situated in water and separated by layers of water from the interface is spontaneously adsorbed onto the tricaprylin surface during MD simulation. The opening and closing motions of the lid are simulated by PaCS-MD and subsequent MSM analysis provided the free energy landscape and time scale of the conformational transitions among the closed, semi-open, and open states. The closed state is the most stable in the water system but the stable conformation in the interface system shifts to the semi-open state. In the interface system, the transition probability to the open state is higher than in the water system. These effects could explain the energetics and kinetics origin of previously reported interfacial activation of CALB. We also suggest two types of mechanisms for substrate binding in which small and hydrophilic substrates bind without interfacial activation while large and bulky substrates bind via interfacial activation. These findings could help expand the application of CALB towards a wide variety of substrates.

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Utilization of discard bovine bone as a support for immobilization of recombinant Rhizopus oryzae lipase expressed in Pichia pastoris

Cited by 4 publications

References 36 publications

Recent advances on sources and industrial applications of lipases

Recent advances on sources and industrial applications of lipases

Energetic and Kinetic Origins of CALB Interfacial Activation Revealed by PaCS-MD/MSM

Energetic and Kinetic Origin of CALB Interfacial Activation Revealed by PaCS-MD/MSM

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