Investigating the structural and functional consequences of circular permutation on lipase B from Candida antarctica.
AuthorsQian Z, Fields CJ, Lutz S,
JournalChembiochem
PubMed ID17876754
'The engineering of lipase B from Candida antarctica (CALB) by circular permutation has yielded over sixty hydrolase variants, and several show significantly improved catalytic performance. Here we report a detailed characterization of ten selected enzyme variants by kinetic and spectroscopic methods to further elucidate the impact of circular permutation on ... More
Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution.
AuthorsZhang N, Suen WC, Windsor W, Xiao L, Madison V, Zaks A
JournalProtein Eng
PubMed ID12968077
'To expand the functionality of lipase B from Candida antarctica (CALB) we have used directed evolution to create CALB mutants with improved resistance towards irreversible thermal inactivation. Two mutants, 23G5 and 195F1, were generated with over a 20-fold increase in half-life at 70 degrees C compared with the wild-type CALB ... More
Improved triglyceride transesterification by circular permuted Candida antarctica lipase B.
AuthorsYu Y, Lutz S,
JournalBiotechnol Bioeng
PubMed ID19609971
Lipases represent a versatile class of biocatalysts with numerous potential applications in industry including the production of biodiesel via enzyme-catalyzed transesterification. In this article, we have investigated the performance of cp283, a variant of Candida antarctica lipase B (CALB) engineered by circular permutation, with a series of esters, as well ... More
Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity.
Pancreatic lipase-related protein 2 (PLRP2) is induced by IL-4 in vitro in cytotoxic T lymphocyte (CTL) clones and CTLs from immunized wild-type (WT) PLRP2(+/+) are more cytotoxic than PLRP2(-/-) CTLs, suggesting to previous investigators that the lipase PLRP2 might support CTL functions. Here, we further evaluate PLRP2 in CTLs. We ... More
A novel glucan-binding protein with lipase activity from the oral pathogen Streptococcus mutans.
AuthorsShah DS, Russell RR
JournalMicrobiology
PubMed ID15184580
Streptococcus mutans produces extracellular glucosyltransferases (GTFs) that synthesize glucans from sucrose. These glucans are important in determining the permeability properties and adhesiveness of dental plaque. GTFs and the GbpA glucan-binding protein are characterized by a binding domain containing a series of 33-amino-acid repeats, called 'A' repeats. The S. mutans genome ... More