Perspectives and industrial potential of PGA selectivity and promiscuity

Grulich, Michal; Štěpánek, Václav; Kyslı́k, Pavel

doi:10.1016/j.biotechadv.2013.07.005

Cited by 33 publications

(18 citation statements)

References 162 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The reactions, which were used for the synthesis of (hetero)spiro [5.5] undecane derivatives produced the cis isomers in all the cases. Grulich et al [70] provide a useful summary of the applications of Penicillin G acylases which are known to catalyse transesterifications, Markonikov additions or Henry reactions. Unfortunately, the catalytic efficiency reported so far in these promiscuous reactions is far from satisfactory for any biotechnological applications.…”

Section: Catalytic Promiscuity: Beyond Lipasesmentioning

confidence: 99%

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Arora

Mukherjee

Gupta

2014

Sustain Chem Process

View full text Add to dashboard Cite

Enzyme promiscuity can be classified into substrate promiscuity, condition promiscuity and catalytic promiscuity. Enzyme promiscuity results in far larger ranges of organic compounds which can be obtained by biocatalysis. While early examples mostly involved use of lipases, more recent literature shows that catalytic promiscuity occurs more widely and many other classes of enzymes can be used to obtain diverse kinds of molecules. This is of immense relevance in the context of white biotechnology as enzyme catalysed reactions use greener conditions.

show abstract

Section: Catalytic Promiscuity: Beyond Lipasesmentioning

confidence: 99%

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Arora

Mukherjee

Gupta

2014

Sustain Chem Process

View full text Add to dashboard Cite

show abstract

“…Many authors have reviewed the use of penicillin acylases in the pharmaceutical industry, and the methods used to improve the process economics, including mutagenesis, protein engineering, enzyme production and immobilization and advancements during downstream processing (Arroyo et al, 2003;Chandel et al, 2008;Grulich, 2013;Parmar et al, 2000;Shewale & Sudhakaran, 1997;Sio & Quax, 2004). However, the importance of these enzymes in the industrial arena has overshadowed the preliminary efforts to study their biological role in the natural metabolism of the microorganisms that produce them.…”

Section: Introductionmentioning

confidence: 97%

Penicillin acylases revisited: importance beyond their industrial utility

Avinash

Pundle

Ramasamy

et al. 2014

Critical Reviews in Biotechnology

View full text Add to dashboard Cite

It is of great importance to study the physiological roles of enzymes in nature; however, in some cases, it is not easily apparent. Penicillin acylases are pharmaceutically important enzymes that cleave the acyl side chains of penicillins, thus paving the way for production of newer semi-synthetic antibiotics. They are classified according to the type of penicillin (G or V) that they preferentially hydrolyze. Penicillin acylases are also used in the resolution of racemic mixtures and peptide synthesis. However, it is rather unfortunate that the focus on the use of penicillin acylases for industrial applications has stolen the spotlight from the study of the importance of these enzymes in natural metabolism. The penicillin acylases, so far characterized from different organisms, show differences in their structural nature and substrate spectrum. These enzymes are also closely related to the bacterial signalling phenomenon, quorum sensing, as detailed in this review. This review details studies on biochemical and structural characteristics of recently discovered penicillin acylases. We also attempt to organize the available insights into the possible in vivo role of penicillin acylases and related enzymes and emphasize the need to refocus research efforts in this direction.

show abstract

“…3.5.1.11) is a vital hydrolase widely used for the synthesis of 6-aminopenicillanic acid (6-APA) and b-lactam antibiotics in the pharmaceutical industry, 31,32 which is very suitable for catalytic performance studies. 3.5.1.11) is a vital hydrolase widely used for the synthesis of 6-aminopenicillanic acid (6-APA) and b-lactam antibiotics in the pharmaceutical industry, 31,32 which is very suitable for catalytic performance studies.…”

Section: Introductionmentioning

confidence: 99%

MOF-templated rough, ultrathin inorganic microcapsules for enzyme immobilization

et al. 2015

View full text Add to dashboard Cite

Ultrathin titania microcapsules with rough surfaces were prepared by using a metal-organic framework (ZIF-8) as one kind of hard template to mediate the structures of the microcapsule shell. Specifically, CaCO 3 particles were first coated with tannic acid (TA) followed by the deposition of hydrophobic ZIF-8 and another TA layer, the obtained particles were then assembled with protamine/TiO 2 bilayers through biomimetic mineralization. Finally, the microcapsules (Z-TiO 2 ) were obtained after simultaneously removing CaCO 3 and ZIF-8 templates using ethylenediaminetetraacetic acid (EDTA). The coordination interaction between TA and ZIF-8 ensured the robust templating which endowed the microcapsules with a rough surface and an ultrathin microcapsules shell (100 nm) with 4.4 nm pore size. Moreover, the surface roughness of microcapsules can be regulated by changing the size of ZIF-8 crystals. The microcapsules were then utilized to immobilize penicillin G acylase (PGA). And PGA@Z-TiO 2 retained 69% activity of equivalent free PGA with a loading capacity of 160 mg g À1 . The PGA@Z-TiO 2 microcapsules exhibited superior reusability: after recycling 8 times, the conversion of the enzymatic reaction remained 36.0%, which was twice higher than that of PGA@TiO 2 (14.7%). Moreover, compared with free PGA and PGA@TiO 2 microcapsules, PGA@Z-TiO 2 microcapsules exhibited higher thermal and storage stability. After storing for 60 days, the relative activity of PGA@Z-TiO 2 remained 89.6%, which was higher than that of free PGA (34.5%) and PGA@TiO 2 (73.6%). ZIF-8 can be envisioned to be a novel class of hard template for preparing a broad variety of microcapsules with different hierarchical structures. † Electronic supplementary information (ESI) available: SEM and TEM images of ZIF-8 particles, nitrogen adsorption-desorption isotherms of ZIF-8 particles, and UV-vis spectra of the assembled multilayer film. See Fig. 12 Recycling stability of PGA@Z-TiO 2 and PGA@TiO 2 (a), temperature stability (b), pH stability (c), and storage stability (d) of free PGA, PGA@Z-TiO 2 and PGA@TiO 2 MCs.

show abstract

Perspectives and industrial potential of PGA selectivity and promiscuity

Cited by 33 publications

References 162 publications

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Penicillin acylases revisited: importance beyond their industrial utility

MOF-templated rough, ultrathin inorganic microcapsules for enzyme immobilization

Contact Info

Product

Resources

About