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1.
Polymers (Basel) ; 13(7)2021 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-33808084

RESUMO

The thermal insulation of buildings using wood fiber insulation boards (WFIBs) constitutes a positive contribution towards climate change. Thereby, the bonding of wood fibers using mainly petrochemical-based resins such as polymeric diphenylmethane diisocyanate (pMDI) is an important measure to meet required board properties. Still there is a need to reduce or partial substitute the amount of these kinds of resins in favor of a greener product. This study therefore focusses on the feasibility of reducing the amount of pMDI by 50% through the addition of 1% BioPiva 395 or Indulin as two types of softwood Kraft-Lignin and lignin rich canola hulls together with propylene carbonate as a diluent. A panel density of 160 kg/m3 and a thickness of 40 mm was aimed. The curing of these modified pMDI was investigated by using two types of techniques: hot-steam (HS) and innovative hot-air/hot-steam-process (HA/HS). The WFIBs were then tested on their physical-mechanical properties. The equilibrium moisture content (EMC) was determined at two different climates. An exemplary investigation of thermal conductivity was conducted as well. The WFIBs did undergo a further chemically based analysis towards extractives content and elemental (C, N) composition. The results show that it is feasible to produce WFIBs with lower quantities of pMDI resin and added lignin with enhanced physical-mechanical board properties, which were lacking no disadvantages towards thermal conductivity or behavior towards moisture, especially when cured via HA/HS-process.

2.
Front Bioeng Biotechnol ; 9: 788622, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-35155404

RESUMO

Laccase-mediator-oxidized lignin offers replacement for conventional chemical binders to produce fiberboards. Compared to the previously reported laccase-mediator system (LMS), a lignin-laccase-mediator-system (LLMS) has an advantage in that it requires much shorter fiber-enzyme incubation time due to significantly increased redox reactions. However, the cost of regularly applying laccase on an industrial scale is currently too high. We have employed CcLcc5 from cultures of the basidiomycete Coprinopsis cinerea as a novel basi-laccase (a CAZy subfamily AA1_1 laccase) in medium-density fiberboard (MDF) production, in comparison to the commercial formulation Novozym 51003 with recombinantly produced asco-laccase MtL (a CAZy subfamily AA1_3 laccase-like multicopper oxidase from the ascomycete Myceliophthora thermophila). With the best-performing natural mediator 2,6-dimethoxyphenol (DMP), unpurified CcLcc5 was almost as good as formulated Novozym 51003 in increasing the molecular weight (MW) of the technical lignins tested, the hydrophilic high-MW Ca-lignosulfonate and the hydrophobic low-MW kraft lignin (Indulin AT). Oxygen consumption rates of the two distantly related, poorly conserved enzymes (31% sequence identity) with different mediators and lignosulfonate were also comparable, but Indulin AT significantly reduced the oxidative activity of Novozym 51003 unlike CcLcc5, regardless of the mediator used, either DMP or guaiacol. Oxygen uptake by both laccases was much faster with both technical lignins with DMP than with guaiacol. In case of lignosulfonate and DMP, 20-30 min of incubation was sufficient for full oxygen consumption, which fits in well in time with the usual binder application steps in industrial MDF production processes. LLMS-bonded MDF was thus produced on a pilot-plant scale with either crude CcLcc5 or Novozym 51003 at reduced enzyme levels of 5 kU/kg absolutely dry wood fiber with lignosulfonate and mediator DMP. Boards produced with CcLcc5 were comparably good as those made with Novozym 51003. Boards reached nearly standard specifications in internal bond strength (IB) and modulus of rupture (MOR), while thickness swelling (TS) was less good based on the hydrophilic character of lignosulfonate. LLMS-bonded MDF with Indulin AT and DMP performed better in TS but showed reduced IB and MOR values.

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