Polyesters from Macrolactones Using Commercial Lipase NS 88011 and Novozym 435 as Biocatalysts

Abstract

The demand for environmentally friendly products allied with the depletion of natural resources has increased the search for sustainable materials in chemical and pharmaceutical industries. Polyesters are among the most widely used biodegradable polymers in biomedical applications. In this work, aliphatic polyesters (from globalide and ω-pentadecalactone) were synthesized using a new commercial biocatalyst, the low-cost immobilized NS 88011 lipase (lipase B from Candida antarctica immobilized on a hydrophobic support). Results were compared with those obtained under the same conditions using a traditional, but more expensive, commercial biocatalyst, Novozym 435 (lipase B from C. antarctica immobilized on Lewatit VP OC). When NS 88011 was used in the polymerization of globalide, longer reaction times (240 min)-when compared to Novozym 435-were required to obtain high yields (80-90 wt%). However, higher molecular weights were achieved. When poly(ω-pentadecalactone) was synthesized, high yields and molecular weights (130,000 g mol) were obtained and the enzyme concentration showed strong influence on the polyester properties. This is the first report describing NS 88011 in polymer synthesis. The use of this cheaper enzymatic preparation can provide an alternative for polyester synthesis via enzymatic ring-opening polymerization.

Novozym 435: the “perfect” lipase immobilized biocatalyst?

“…363 N435 exhibited better activity than NS 88011 (a commercial product also from CALB) in the production of aliphatic polyesters using globalide and ω-pentadecalactone as substrates, although the length of the polymer was smaller. 364 PolyIJε-caprolactone) has been synthesized via ring-opening polymerization of ε-caprolactone catalyzed by N435 in ionic liquids. 365 Other polymers are based on 2,5-furandicarboxylic acid.…”

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

“…As a clear example of the simplicity and usefulness of this immobilization protocol, Novozym 435, that is the immobilized form of the lipase B from Candida antarctica and very likely the most utilized commercial immobilized biocatalysts, has been prepared using this strategy employing Lewatit VP OC 1600 as support (Bansode et al, 2017;Du et al, 2004;Endo et al, 2018;Galgali et al, 2018;Kaar et al, 2003;Ortiz et al, 2019;Polloni et al, 2017;Sbardelotto et al, 2018;Zhang et al, 2018). Table 1 shows a compilation of the most utilized hydrophobic supports and the lipases that have been immobilized on them (from 2010 until present).…”

Copolymacrolactones Grafted with l-Glutamic Acid: Synthesis, Structure, and Nanocarrier Properties

“…The results obtained in these copolymerizations are shown in Table 1. The eROP method, previously used for the homopolymerization of both Gl and PDL [23][24][25], has afforded satisfactory results in the copolymerization of these two MLs with yields between 75% and 90% and copolymer compositions showing small deviations with respect to feed compositions. The copolymerization of 6-hexadecenlactone and PDL described recently by Pappalardo et al [22] carried out in the presence of a pyridylamidozinc(II) complex rendered copolymers with essentially the same compositions as that of their feeds.…”