Purification and identification of an angiotensin I-converting enzyme inhibitory peptide from cauliflower by-products protein hydrolysate

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Purification and identification of an angiotensin I-converting enzyme inhibitory peptide from cauliflower by-products protein hydrolysate

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作者：Yang Xu^a ; ^{yangxu93@zju.edu.cn" class="auth_mail" title="E-mail the corresponding author} ; Tao Bao^a ; ^{taobao@zju.edu.cn" class="auth_mail" title="E-mail the corresponding author} ; Wen Han^a ; ^{xubajing@163.com" class="auth_mail" title="E-mail the corresponding author} ; Wei Chen^a ; ^{hongmingsu@zju.edu.cn" class="auth_mail" title="E-mail the corresponding author} ; Xiaodong Zheng^a ; ^{xdzhengzju@126.com" class="auth_mail" title="E-mail the corresponding author} ; Jianxu Wang^b ; ^{wjx3729806@163.com" class="auth_mail" title="E-mail the corresponding author}
关键词：Cauliflower by-products protein ; Enzymatic hydrolysis ; ACE inhibitory peptide ; Purification and identification
刊名：Process Biochemistry
出版年：2016
出版时间：September 2016
年：2016
卷：51
期：9
页码：1299-1305
全文大小：1203 K

文摘

•: Alcalase hydrolysate exhibited the highest ACE inhibitory activity.
•: An ACE inhibitory peptide (Val-Trp) was isolated and identified.
•: This peptide had a potent ACE inhibitory activity with an IC₅₀ value of 31.30 μM.
•: About 42 mg of dipeptide was obtained from 1 kg of fresh Cauliflower by-products.

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