Immobilization of Neutral Protease from Bacillus subtilis for Regioselective Hydrolysis of Acetylated Nucleosides: Application to Capecitabine Synthesis

  title={Immobilization of Neutral Protease from Bacillus subtilis for Regioselective Hydrolysis of Acetylated Nucleosides: Application to Capecitabine Synthesis},
  author={Teodora Bavaro and Giulia Cattaneo and Immacolata Serra and Ilaria Benucci and Massimo Pregnolato and Marco Terreni},
This paper describes the immobilization of the neutral protease from Bacillus subtilis and its application in the regioselective hydrolysis of acetylated nucleosides, including building blocks useful for the preparation of anticancer products. Regarding the immobilization study, different results have been obtained depending on the immobilization procedure. Epoxy hydrophobic carriers gave a poorly stable derivative that released almost 50% of the immobilized protein under the required reaction… 
Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications
In this paper, we describe the development of an efficient enzyme immobilization procedure based on the activation of epoxy carriers with glucosamine. This approach aims at both creating a
Immobilization of enzymes and their use in biotechnological applications
Abstract Although enzymes are becoming increasingly important tools in biotechnological applications, their use is limited. This limitation is due to their sensitivity to the environment of the
Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes
The results demonstrate that the use of co-immobilised enzymes holds promise as an industrial strategy for producing low lactose milk to benefit people with lactose intolerance.
A new bacillolycin with serin-protease nature is inhibited by cupper
Abstract In this study, it is aimed to search for new proteases with novel properties from bacteria and to characterise the properties of the enzyme. The best protease producing microorganisms was
N-Lipidated Amino Acids and Peptides Immobilized on Cellulose Able to Split Amide Bonds
It has been found that incorporation of metal ions into catalytic pockets increase the activity of the synzymes and catalytic activity gradually diminished after subsequent re-use.
Bamboo (Phyllostachys pubescens) as a Natural Support for Neutral Protease Immobilization
Compared to FNP, INP showed broader thermal and storage stability under the same trial condition, and presented considerable recycling efficiency for up to six consecutive cycles, which demonstrated that INP presented higher affinity to substrate.
Immobilization of γ‐Glutamyl Transpeptidase from Equine Kidney for the Synthesis of kokumi Compounds
γ‐Glutamyl transpeptidase from equine kidney (ekGGT, E.C. is an intrinsic membrane enzyme which transfers the γ‐glutamyl moiety of glutathione to amino acids and peptides, thus producing
Developing a Library of Mannose-Based Mono- and Disaccharides: A General Chemoenzymatic Approach to Monohydroxylated Building Blocks
A small library of differently monohydroxylated building blocks that could be used as intermediates for the synthesis of mannosylated glycoconjugate vaccines targeting mannose receptors of antigen presenting cells is prepared.
Multi-enzymatic Systems Immobilized on Chitosan Beads for Pomegranate Juice Treatment in Fluidized Bed Reactor: Effect on Haze-Active Molecules and Chromatic Properties
In this study, two different food-grade enzymes (i.e., bromelain from a pineapple stem (protease) and Pectinex® BE XXL (pectinase)) were successfully immobilized on chitosan beads and their
Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
Bioconjugates based on hEGF mimicking the protein in its native state and thus suitable for tissue engineering applications, in particular for treating skin-related disorders as burns are developed.


Stabilization of thymidine phosphorylase from Escherichia coli by immobilization and post immobilization techniques.
Homodimeric thymidine phosphorylase from Escherichia coli was immobilized on solid support with the aim to have a stable and recyclable biocatalyst for nucleoside synthesis to obtain an active catalyst which resulted up to 6-fold and 3-fold more stable than the soluble (non immobilized) enzyme and the just adsorbed (non cross-linked) counterpart, respectively, at pH 10 and 37°C.
Recombinant lipase from Candida rugosa for regioselective hydrolysis of peracetylated nucleosides. A comparison with commercial non-recombinant lipases
Abstract Commercial lipases from the yeast Candida rugosa have been compared with two recombinant C. rugosa lipases, rCRL1 and rCRL1lid3, with respect to their immobilization and exploitation in
Protein hydrolysis by immobilized and stabilized trypsin
Analysis of the three‐dimensional (3D) structure of the best immobilized trypsin derivative showed a surface region containing two amino terminal groups and five lysine (Lys) residues that may be responsible for this novel and interesting immobilization and stabilization.
Characterization and study of the orientation of immobilized enzymes by tryptic digestion and HPLC-MS: design of an efficient catalyst for the synthesis of cephalosporins.
The results indicate that PGA immobilization on both supports is partially unfavorable, driving the active site near the support surface, and this type of orientation of the enzyme enhances the effect of the nature of the support and of the binding chemistry on the catalytic properties.
Modulation of the Microenvironment Surrounding the Active Site of Penicillin G Acylase Immobilized on Acrylic Carriers Improves the Enzymatic Synthesis of Cephalosporins
The catalytic properties of penicillin G acylase (PGA) from Escherichia coli in kinetically controlled synthesis of β-lactam antibiotics are negatively affected upon immobilization on hydrophobic
Purification and improvement of the functional properties of Rhizopus oryzae lipase using immobilization techniques
Abstract The adsorption/immobilization of Rhizopus oryzae lipase (ROL) has permitted the development of several strategies to improve the properties of this industrial enzyme. The enzyme can be
Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases
A relation between the influence of immobilization on the improvement of the properties of selected oxidoreductases and their commercial value is presented and the role that different immobilization methods play in the reduction of enzyme inhibition during biotechnological processes is presented.
A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
These results suggest that lipases recognize these "well-defined" hydrophobic supports as solid interfaces and they become adsorbed through the external areas of the largeHydrophobic active centers of their "open and hyperactivated structure", which becomes a very promising immobilization method with general application for most lipases.
Immobilization of enzymes on heterofunctional epoxy supports
“tailor-made” heterofunctional epoxy supports are designed and the performance of the immobilization protocols are described here.
Microbiology and Industrial Biotechnology of Food-Grade Proteases: A Perspective
This review tracks the developments in the field of acidic and neutral protease production with regard to the producers, methods of production and their improvement, the product and its applications.