Harnessing Ogataea parapolymorpha DL-1 alcohol oxidase in Komagataella phaffii for recombinant xylanase expression

Xylanase production attracted attention because it was an important biological macromolecular in food industry, pharmaceutical industry, animal feed, biorefinery industry. Komagataella phaffii, as a famous recombinant protein producer, used alcohol oxidase 1 to oxidize methanol for recombinant xylanase expression. However, low affinity of alcohol oxidase 1 to oxygen was considered as a limitation because of requirement of a large amount oxygen supply, resulting low consumption of methanol. In this study, Ogataea parapolymorpha DL-1 alcohol oxidase (OpAOX) was used to substitute K. phaffii alcohol oxidase 1 for recombinant xylanase expression increment by 26.7°% through increasing specific methanol consumption rate. Furtherly, recombinant xylanase expression increased by 44.5°% after pH adjustment. These results were also verified by recombinant green fluorescent protein expression in this K. phaffii strain with 54.3°% increment. Therefore, K. phaffii harboring OpAOX provided new approach of recombinant xylanse production, and demonstrated a general strategy for other food related by-products production by K. phaffii.