Article
Biochemistry & Molecular Biology
Federico Zappaterra, Maria Elena Maldonado Rodriguez, Daniela Summa, Bruno Semeraro, Stefania Costa, Elena Tamburini
Summary: This study investigates the enzymatic esterification of ibuprofen to improve its solubility as a strategy for hydrophilization. The covalent attack of highly hydrophilic molecules using commercially available bioactive compounds was proposed. Using porcine pancreas lipase (PPL) as a biocatalyst, the esterification of ibuprofen in a hexane/water biphasic system was optimized for effective production of the IBU-sorbitol ester.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Naba Kumar Kalita, Minna Hakkarainen
Summary: A green strategy was demonstrated to accelerate the biodegradation rate of cellulose acetate (CA) through deacetylation. The immobilization of lipase from Candida rugosa on CA particles resulted in significant deacetylation, as evidenced by changes in molecular weight and water contact angle. This approach showed promising potential for developing modified lignocellulose materials with retained biodegradability.
Article
Green & Sustainable Science & Technology
Aysha Al Qayoudi, Sulaiman Al-Zuhair
Summary: Immobilization of enzymes has been proposed as a method to simplify their separation and reuse, but it also leads to additional diffusion limitations that fully utilize enzyme activity. This study focuses on the immobilization of lipase on zeolite and its application in oil hydrolysis. The Sips model is identified as the best description for the adsorption process, and the zeolite's adsorption capacity is determined to be 62.6 mg/g. The experimental results of enzymatic hydrolysis of olive oil using the immobilized lipase show that both surface reaction and diffusion have significant effects.
Article
Chemistry, Physical
Esra Bilgin Simsek, Didem Saloglu
Summary: This study successfully immobilized different types of lipases on g-C3N4, obtaining biohybrid catalysts with high immobilization yields through physical adsorption and covalent bonding methods. The immobilized lipases showed higher kinetic constant values, and the photocatalytic efficiency of the biohybrid catalysts was also superior to raw g-C3N4.
JOURNAL OF MOLECULAR LIQUIDS
(2021)
Review
Chemistry, Applied
Li-Cheng Yang, Heping Deng, Hans Renata
Summary: This article summarizes the chemoenzymatic and biocatalytic methodologies for DKR developed in the past decade, highlighting their applications in the preparation of active pharmaceutical ingredients and emerging paradigms.
ORGANIC PROCESS RESEARCH & DEVELOPMENT
(2022)
Review
Chemistry, Multidisciplinary
Max Lubberink, William Finnigan, Sabine L. Flitsch
Summary: Amide bonds are commonly formed in the pharmaceutical industry and there is a growing interest in biocatalytic methods for their synthesis. The use of low water systems and ATP-dependent enzymes have shown promise in driving amide bond formation. A publicly available database, RetroBioCat, has been compiled to provide literature on these methods.
Article
Chemistry, Multidisciplinary
Suraksha Gahalawat, Yesu Addepalli, Stephen P. Fink, Lakshmi Kasturi, Sanford D. Markowitz, Joseph M. Ready
Summary: Various functionalized sulfinyl esters can be synthesized through a series of chemical reactions, and enzymatic resolution can efficiently provide enantiopure sulfinyl esters.
CHEMISTRY-A EUROPEAN JOURNAL
(2023)
Article
Chemistry, Physical
Giulia Roxana Gheorghita, Victoria Ioana Paun, Simona Neagu, Gabriel-Mihai Maria, Madalin Enache, Cristina Purcarea, Vasile I. Parvulescu, Madalina Tudorache
Summary: Extremophilic biocatalysts, such as cold-active lipases, have been successfully integrated into industrial applications for enhanced catalytic performance. Utilizing various immobilization techniques, including covalent attachment to nano-/micro-sized magnetic or polymeric resin beads, has resulted in bio-composites with similar or even higher catalytic activity under cold conditions. The developed immobilized biocatalysts show promising potential for efficient biocatalytic modification processes.
Article
Chemistry, Applied
Bruna G. Palma, Raquel A. C. Leao, Rodrigo O. M. A. de Souza, Omar G. Pandoli
Summary: The study using bamboo powder as a support for immobilizing two different biocatalysts in ethyl palmitate synthesis showed that both IB-CalB and IB-RM exhibited good recycling efficiency. IB-CalB demonstrated higher enantioselectivity conversion. The high conversion rate of IB-CalB in enantioselective catalysis under flow mode regime indicates the potential of a simple and cost-effective enzyme adsorption method for industrial biocatalytic transformation.
Article
Chemistry, Multidisciplinary
Itoh Toshiyuki
Summary: The use of ILs as solvents and stabilizers for enzymes, specifically lipases, allows for the recyclable use of enzymes, acceleration of transesterification, and enhancement of enzyme stability and reaction activity. This IL engineering approach has a significant impact on lipase-catalyzed reactions and has the potential to improve enzyme capabilities.
Article
Chemistry, Organic
Mansour Shahedi, Niloofar Omidi, Zohreh Habibi, Maryam Yousefi, Jesper Brask, Behrouz Notash, Mehdi Mohammadi
Summary: Highly functionalized pyrrolidine-2,3-diones were efficiently and stereoselectively synthesized via a biocatalytic approach. The reaction involved the oxidation of catechols to ortho-quinones using Myceliophthora thermophila laccase (Novozym 51003), followed by 1,4-addition with 3-hydroxy-1,5-dihydro-2H-pyrrol-2-ones to form all-carbon quaternary stereocenters. The reaction yielded 13 products with moderate to good yields (42-91%) when various substituents were used on both reactants. In contrast, only one reaction resulted in a product (60% yield) when K3Fe(CN)(6) was used as a catalyst.
ORGANIC & BIOMOLECULAR CHEMISTRY
(2023)
Article
Biochemistry & Molecular Biology
Jian Ou, Xin Yuan, Yu Liu, Panliang Zhang, Weifeng Xu, Kewen Tang
Summary: Immobilizing Pseudomonas cepacia lipase (PCL) into Zeolitic imidazolate framework-8 (ZIF-8) through physical adsorption can enhance enzyme activity and stability. The immobilized enzyme shows superior performance in enantioselective hydrolysis and transesterification reactions, with good reusability.
PROCESS BIOCHEMISTRY
(2021)
Article
Chemistry, Physical
Heitor B. S. Bento, Cristiano E. R. Reis, Pedro A. Pinto, Daniela V. Cortez, Renata N. Vilas Boas, Tales A. Costa-Silva, Ana K. F. Carvalho, Heizir F. de Castro
Summary: This study focused on immobilizing commercial lipase onto magnetic particles for the synthesis of biodiesel, showing improved thermal stability and esterification activity. The immobilized system demonstrated high productivity and met the quality requirements of biodiesel fuel standards under continuous operation.
Article
Biotechnology & Applied Microbiology
Yalda Amini, Mansour Shahedi, Zohreh Habibi, Maryam Yousefi, Maryam Ashjari, Mehdi Mohammadi
Summary: A new method was used to immobilize three lipases on amine-functionalized magnetic nanoparticles. The immobilization process was simple and fast, resulting in high immobilization yields. The immobilized lipases were used for biodiesel production from waste cooking oil, and the production conditions were optimized using response surface methodology.
BIORESOURCES AND BIOPROCESSING
(2022)
Article
Chemistry, Physical
Le Zhong, Yuxiao Feng, Hongtong Hu, Jiabao Xu, Ziyuan Wang, Yingjie Du, Jiandong Cui, Shiru Jia
Summary: In this study, the hydrophobic ZIF-L coated with PDMS was successfully used to immobilize lipase from Aspergillus oryzae, enhancing its stability and activity recovery. The immobilized lipase exhibited better storage stability and catalyzed higher biodiesel yield, showing great potential for biodiesel production.
JOURNAL OF COLLOID AND INTERFACE SCIENCE
(2021)
