Implementation and use of cloud-based electronic lab notebook in a bioprocess engineering teaching laboratory

Abstract Background Electronic lab notebooks (ELNs) are better equipped than paper lab notebooks (PLNs) to handle present-day life science and engineering experiments that generate large data sets and require high levels of data integrity. But limited training and a lack of workforce with ELN knowledge have restricted the use of ELN in academic and industry research laboratories which still rely on cumbersome PLNs for recordkeeping. We used LabArchives, a cloud-based ELN in our bioprocess engineering lab course to train students in electronic record keeping, good documentation practices (GDPs), and data integrity. Results Implementation of ELN in the bioprocess engineering lab course, an analysis of user experiences, and our development actions to improve ELN training are presented here. ELN improved pedagogy and learning outcomes of the lab course through stream lined workflow, quick data recording and archiving, and enhanced data sharing and collaboration. It also enabled superior data integrity, simplified information exchange, and allowed real-time and remote monitoring of experiments. Several attributes related to positive user experiences of ELN improved between the two subsequent years in which ELN was offered. Student responses also indicate that ELN is better than PLN for compliance. Conclusions We demonstrated that ELN can be successfully implemented in a lab course with significant benefits to pedagogy, GDP training, and data integrity. The methods and processes presented here for ELN implementation can be adapted to many types of laboratory experiments

Medium optimization for chitinase production from Trichoderma virens using central composite design

Medium development for chitinase production by Trichoderma virens was first carried out using conventional method of one-factor-at-a-time. The medium was further optimized using Central Composite Design in which response surface was generated later from the derived model. An experimental design of four variables including various initial pH values, chitin, ammonium sulphate, and methanol concentrations were created using Design Expert® Software, Version 6.0. The design consists of 30 experiments, which include 6 replicates at center points. The optimal value for each variable are 3.0 g/L, chitin; 0.1 g/L, ammonium sulphate; 0.4% (v/v), methanol; and initial pH, 4.0 with predicted chitinase activity of 0.1495 U/mL. These predicted parameters were tested in the laboratory and the final chitinase activity obtained was 0.1471 U/mL, which is almost reaching the predicted value. The optimal medium design showed an improvement of chitinase activity of 80.9% compared to activity obtained from the original Absidia medium composition

Influence of agitation speeds and aeration rates on the Xylanase activity of Aspergillus niger SS7

In this study, the effect of agitation and aeration rates on xylanase activity of Aspergillus niger SS7 in 3-litre stirred tank bioreactor was investigated. The agitation rates tested were 100, 200 and 300 rpm at each airflow rates of 0.5, 1.0 and 1.5 vvm. The maximum xylanase activity in mono- agitator system was at the agitation speed of 200 rpm and aeration rate of 1.0 vvm. In bi-agitator system, at low agitation speed (100 rpm), the xylanase activity was enhanced by 13% compared to mono- agitator system for an aeration rate of 1.0 vvm. Xylanase productivity in continuous culture was higher by approximately 3.5 times than in batch culture

Biocatalysts: Isolation, identification, and immobilization of thermally stable lipase onto three novel biopolymeric supports

Lipase, one of the most important and versatile industrial enzymes, has been isolated, identified, and immobilized onto three novel supports prepared based on our US patent (US20110076737). Nine fungal isolates were cultivated, and maximum lipase activity of 285 U/mL was achieved from the fungal isolate identified as Rhizopus oryzae GF1. The enzyme was shown to be thermally stable at 50 C for 210 min. Three different environmentally friendly biopolymers prepared according to our US patent have been used to immobilize covalently the lipase from Rhizopus oryzae GF1. The structures of the gel beads; grafted alginate, carrageenan and alginate-carrageenan; have been proved by the FTIR. The best formulation, alginate-carrageenan, covalently immobilized 183.5 U/g lipase and was further optimized to load 223 U/g lipase. The immobilization process increased the operational temperature from 30 to 50 C compared to the free enzyme. The hydrolysis of oil using the free and the immobilized lipase was achieved at the same time, 90 min, which reflects no diffusion limitation. The shelf stability showed that the immobilized enzyme retained full activity for over 9 weeks at 4 C, whereas the free enzyme lost 80% of its initial activity after 4 weeks. The reusability test proved the durability of the grafted beads for 20 cycles with a retention of 97% of the immobilized enzyme activity compared to 23% by other authors after the 10th use. © 2013 American Chemical Society