Skip To Main Content
Barindra Sana on Muck Rack

Barindra Sana

As seen in: Wiley Online Library, MDPI, Royal Society of Chemistry, BioRxiv, The Journal of Biological Chemistry
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with Barindra

Contact Barindra, search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Modulation of Ideonella sakaiensis PETase active site flexibility and activity on morphologically distinct substrates by surface charge engineering

|
By Ke Ding, Zarina Levitskaya, Barindra Sana, Rupali Reddy Pasula
| BioRxiv
Abstract Enzymatic hydrolysis of polyethylene terephthalate (PET) waste is a compelling strategy for environmentally friendly recycling of a major pollutant. Here, we investigate the effects of surface charge point mutations both proximal and distal to the active site of the mesophilic PET-degrading enzyme from Ideonella sakaienses (IsPETase) and an engineered thermostable variant with superior activity, STAR PETase.
Open in Who Shared Issue with article?

Phosphate Functionalized Nonisocyanate Polyurethanes with Bio-origin, Water Solubility and Biodegradability

|
By Eric Tam, Ning Chong, Barindra Sana, Choong Ping Sen
| Royal Society of Chemistry Verified
Phosphate Functionalized Nonisocyanate Polyurethanes with Bio-origin, Water Solubility and Biodegradability Nonisocyanate polyurethanes (NIPUs) are an emerging class of polyurethanes produced by circumventing the use of hazardous isocyanates and phosgene in their synthetic route.
Open in Who Shared Issue with article?

Thermostability enhancement of polyethylene terephthalate degrading PETase using self‐ and nonself‐ligating protein scaffolding approaches

|
By Barindra Sana, Research Singapore, Ke Ding, Jia Wei Siau
| Wiley Online Library Verified
2.1 Cloning and mutation The IsPETase gene was codon-optimized for recombinant expression in Escherichia coli and synthesized (IDT). The gene was amplified using primers 1a and 1b (see Supporting Information: Table  for list of oligonucleotide primers). The purified PCR product was cloned with a C-terminus 6-His tag into pET22b vector via NdeI/XhoI using the In-Fusion HD Cloning kit following the manufacturer's protocol (Takara bio). The construct was transformed into chemically competent E.
Open in Who Shared Issue with article?
See all 7 articles