In vitro studies on the degradation of common rubber waste material with the latex clearing protein (Lcp1VH2) of Gordonia polyisoprenivorans VH2.

The enzymatic degradation of the rubber polymer poly(cis-1,4-isoprene), e.g. by the latex clearing protein Lcp1VH2 of Gordonia polyisoprenivorans VH2 has been demonstrated with latex milk or pure isoprene-rubber particles, recently. Unfortunately, carbon black filled vulcanized rubber (CFVR) making the biggest part of worldwide rubber wastes, contains several harmful additives making microbial and enzymatic rubber degradation challenging. However, this study demonstrates the successful enzymatic cleavage of industrially produced CFVR. The formation of the cleavage products, oligo(cis-1,4-isoprenoids), from incubating CFVR particles with Lcp1VH2 was detected by HPLC-MS. Various organic solvents were tested to remove harmful or inhibiting additives like antioxidants to enhance product formation. The pretreatment of CFVR particles, especially with chloroform or cyclohexane, significantly improved the degradation. It was also demonstrated that reducing the particles size and thus increasing the enzymatically accessible surface area of the particles led to a strong acceleration of the degradation process. Furthermore, ATR-IR analyses showed that Lcp1VH2 led to the functionalization of the rubber particle surface with carbonyl groups by cleaving isoprene chains, still linked to the particle. Both, the oligo(cis-1,4-isoprenoids) as well as the functionalized rubber particles, are potentially important products, which can be reused as fine chemicals or as additives in rubber production. The present study, showing the enzymatic degradation of common CFVR for the first time, takes an important step towards a new way of rubber waste disposal and indicates the economic feasibility of an efficient and environmentally friendly recycling process by using the rubber oxygenase Lcp1VH2.