<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pandit, A.</style></author><author><style face="normal" font="default" size="100%">Katkar, V.</style></author><author><style face="normal" font="default" size="100%">Ranade, V.</style></author><author><style face="normal" font="default" size="100%">Bhambure, R.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Real-Time monitoring of biopharmaceutical crystallization: chord length distribution to crystal size distribution for lysozyme, rHu insulin, and vitamin B12</style></title><secondary-title><style face="normal" font="default" size="100%">Industrial and Engineering Chemistry Research</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">This investigation is focused on designing an effective strategy for the real-time monitoring of biopharmaceutical crystallization using focused beam reflectance measurement (FBRM). Lysozyme, rHu insulin, and vitamin B12 were selected as model biopharmaceutical molecules for the study. Under selected experimental conditions, lysozyme exhibits polymorphism with tetragonal and needle-shaped crystals, rHu insulin forms rhombohedral crystals, and vitamin B12 forms polyhedral-shaped crystals. Focused beam reflectance measurements were performed to obtain the real time chord length distribution (CLD) of crystals obtained using static and dynamic conditions. Mathematical models were developed for converting CLD data obtained using FBRM measurements into the useful crystal size distribution (CSD) data for low (tetragonal, rhombohedral and polyhedral) and high aspect ratio crystals (needle). For high-aspect-ratio crystals, both width-based and length-based models were developed for capturing the CSD. The model validation was performed by comparing the model CSD with the CSD obtained using microscopic image analysis. Developed models effectively capture the CSD for variable shape crystals of lysozyme, rHu insulin, and vitamin B12. It was demonstrated that in the case of high-aspect-ratio crystals, there is an intrinsic limitation in using FBRM for length-based crystal size measurement.</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.14</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Halan, V.</style></author><author><style face="normal" font="default" size="100%">Maity, S.</style></author><author><style face="normal" font="default" size="100%">Bhambure, R.</style></author><author><style face="normal" font="default" size="100%">Rathore, A. S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multimodal chromatography for purification of biotherapeutics - a review.</style></title><secondary-title><style face="normal" font="default" size="100%">Current Protein and Peptide Science</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">4-13</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Process chromatography forms the core of purification of biotherapeutics. The unparalleled selectivity that it offers over other alternatives combined with the considerable robustness and scalability make it the unit operation of choice in downstream processing. It is typical to have three to five chromatography steps in a purification process for a biotherapeutic. Generally, these steps offer different modes of separation such as ion-exchange, reversed phase, size exclusion, and hydrophobic interaction. In the past decade, multimodal chromatography has emerged as an alternative to the traditional modes. It involves use of more than one mode of separation and typically combines ion-exchange and hydrophobic interactions to achieve selectivity and sensitivity. Over the last decade, numerous authors have demonstrated the significant potential that multimode chromatography offers as a protein purification tool. This review aims to present key recent developments that have occurred on this topic together with a perspective on future applications of multimodal chromatography.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.696</style></custom4></record></records></xml>