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

IF 4.8 1区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Food Bioscience Pub Date : 2025-03-12 DOI:10.1016/j.fbio.2025.106346

Shoufeng Wang , Wenjie Cong , Mingxuan Wang , Hualan Zhou , Zhenhai Li , Jiguo Wang , Jianguo Zhang

{"title":"Harnessing Ogataea parapolymorpha DL-1 alcohol oxidase in Komagataella phaffii for recombinant xylanase expression","authors":"Shoufeng Wang , Wenjie Cong , Mingxuan Wang , Hualan Zhou , Zhenhai Li , Jiguo Wang , Jianguo Zhang","doi":"10.1016/j.fbio.2025.106346","DOIUrl":null,"url":null,"abstract":"<div><div>Xylanase production attracted attention because it was an important biological macromolecular in food industry, pharmaceutical industry, animal feed, biorefinery industry. <em>Komagataella phaffii</em>, 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, <em>Ogataea parapolymorpha</em> DL-1 alcohol oxidase (<em>Op</em>AOX) was used to substitute <em>K. phaffii</em> 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 <em>K. phaffii</em> strain with 54.3°% increment. Therefore, <em>K. phaffii</em> harboring <em>Op</em>AOX provided new approach of recombinant xylanse production, and demonstrated a general strategy for other food related by-products production by <em>K. phaffii</em>.</div></div>","PeriodicalId":12409,"journal":{"name":"Food Bioscience","volume":"67 ","pages":"Article 106346"},"PeriodicalIF":4.8000,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Bioscience","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S221242922500522X","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

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.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

求助全文

约1分钟内获得全文去求助

来源期刊

Food Bioscience Biochemistry, Genetics and Molecular Biology-Biochemistry

CiteScore

6.40

自引率

5.80%

发文量

671

审稿时长

27 days

期刊介绍： Food Bioscience is a peer-reviewed journal that aims to provide a forum for recent developments in the field of bio-related food research. The journal focuses on both fundamental and applied research worldwide, with special attention to ethnic and cultural aspects of food bioresearch.