Identification and expression patterns of alcohol dehydrogenase genes involving in ester volatile biosynthesis in pear fruit
2017
QIN Gai-hua | QI Xiao-xiao | QI Yong-jie | GAO Zheng-hui | YI Xing-kai | PAN Hai-fa | XU Yi-liu
Alcohol dehydrogenase (ADH) catalyzes the interconversion of aldehydes and their corresponding alcohols, and is a key enzyme in volatile ester biosynthesis. However, little is known regarding ADH and ADH encoding genes (ADHs) in pear. We identified 8 ADHs in the pear’s genome (PbrADHs) by multiple sequences alignment. The PbrADHs were highly homologous in their coding regions, while were diversiform in structure. 9 introns were predicted in PbrADH3–PbrADH8, while 8 introns, generated through exon fusion and intron loss, were predicted in PbrADH1 and PbrADH2. To study the genetic regulation underlying aroma biogenesis in pear fruit, we determined the PbrADH transcripts, ADH activities and volatile contents of fruits during ripening stage for Nanguoli and Dangshansuli, two cultivars having different aroma characteristics. ADH activity was strongly associated with the transcription of ADH6 in the two cultivars during fruit ripening stage. The higher ester content paralleling to a higher ADH activity was detected in Nanguoli than in Dangshansuli, so it is induced that the lower ester content in Dangshansuli fruit may be the result of weak ADH activity. The present study revealed that total ADH activity and volatile ester production correlated with increased PbrADH6 transcript levels. PbrADH6 may contribute to ADH activity catalyzing aldehyde reduction and ester formation in pear fruit.
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