02146nas a2200193 4500008004100000022001400041245014800055210006900203260000900272300001600281490000600297520140000303100002101703700002901724700003001753700002601783700002001809856012301829 2020 eng d a2470-134300aProcess development for 6-aminopenicillanic acid production using lentikats-encapsulated escherichia coli cells expressing penicillin V acylase0 aProcess development for 6aminopenicillanic acid production using cNOV  a28972-289760 v53 a

Penicillin V acylase (PVA, EC 3.5.1.11) hydrolyzes the side chain of phenoxymethylpenicillin (Pen V) and finds application in the manufacture of the pharmaceutical intermediate 6-aminopenicillanic acid (6-APA). Here, we report the scale-up of cultivation of Escherichia coli whole cells expressing a highly active PVA from Pectobacterium atrosepticum and their encapsulation in polyvinyl alcohol-poly(ethylene glycol) Lentikats hydrogels. A biocatalytic process for the hydrolysis of 2% (w/v) Pen V was set up in a 2 L reactor using the Lentikats-immobilized whole cells, with a customized setup to enable continuous downstream processing of the reaction products. The biocatalytic reaction afforded complete conversion of Pen V for 10 reaction cycles, with an overall 90% conversion up to 50 cycles. The bioprocess was further scaled up to the pilot-scale at 10 L, enabling complete conversion of Pen V to 6-APA for 10 cycles. The 6-APA and phenoxy acetic acid products were recovered from downstream processing with isolated yields of 85-90 and 87-92%, respectively. Immobilization in Lentikats beads improved the stability of the whole cells on storage, maintaining 90-100% activity and similar conversion efficiency after 3 months at 4 degrees C. The robust PVA biocatalyst can be employed in a continuous process to provide a sustainable route for bulk 6-APA production from Pen V.

1 aSawant, Amol, M.1 aSunder, Avinash, Vellore1 aVamkudoth, Koteswara, Rao1 aRamasamy, Sureshkumar1 aPundle, Archana uhttp://library.ncl.res.in/content/process-development-6-aminopenicillanic-acid-production-using-lentikats-encapsulated03135nas a2200181 4500008004100000245009600041210006900137260000800206300001400214490000700228520248000235100001902715700002202734700001802756700003002774700002502804856012402829 2022 eng d00aPectinase production by aspergillus niger and its applications in fruit juice clarification0 aPectinase production by aspergillus niger and its applications i cNOV a2724-27370 v163 a

Pectinases (EC 3.2.1.15) are a class of enzymes that catalyze the depolymerization or de-esterification reactions that degrade pectic substances. In the present study, we have isolated the Aspergillus niger strain from soil samples, in India and evaluated pectinase production. The highest pectinase producing A. niger strain was further evaluated and optimized with various agricultural wastes. Plackett-Burman design (PBD) and Central composite design ‘(CCD)’ were used to determine the best parameters for maximum pectinase production. Pectinase activity was increased to 99.21 U/ml after optimizing the production medium using PBD and CCD statistical analysis. A positive correlation of pectinase activity between predicted (112.65 U/ml) and experimental (99.21 U/ml with SD=0.005) optimum was observed. Maximum pectinase was produced by A. niger under submerged fermentation, utilizing orange peel, which is a cost-effective, adaptable, and environmentally friendly approach. The partially purified pectinase showed significant application for apple juice clarification and showed the ability to degrade pectin and therefore the colour change was observed in apple juice within 120 min. Maximum pectinase was produced by A. niger using agricultural waste orange peel under submerged fermentation which is an economical, versatile and eco-friendly process and pectinase showed a significant application for apple juice clarification.

1 aWagh, Vrushali1 aPatel, Hirvitaben1 aPatel, Nafisa1 aVamkudoth, Koteswara, Rao1 aAjmera, Shanthipriya uhttp://library.ncl.res.in/content/pectinase-production-aspergillus-niger-and-its-applications-fruit-juice-clarification