期刊文献+

高温豆粕肽粉的苦味及ACE抑制活性研究 被引量:6

Bitterness and ACE inhibitory activity of the high-temperature soybean meal peptide
下载PDF
导出
摘要 以高温豆粕为原料,Alcalase2.4L酶为催化剂,通过L(934)正交试验,获得制备ACE抑制肽的最佳条件为:底物浓度4%、酶活力1500U/g、pH值8.5、温度50℃,此时ACE抑制活性达到78.85%。在此基础上,采用毛霉蛋白酶酶解3h、6h和1%、2%的β-环糊精(β-CD)包埋进行脱苦处理,试验结果表明,1%的β-CD包埋对高温豆粕酶解液具有最佳的脱苦和最大保存其ACE抑制活性的作用。 Using high-temperature soybean meal as raw materials and Alcalase 2.4L as a catalyst, the optimal conditions of ACE inhibitory activity was obtained using the L9 (34) orthogonal experiment as followed: substrate concentration 4%, enzyme activity 1500U/g, pH value 8.5 and the temperature 50℃. Under these conditions, the high ACE inhibitory activity reached 78.85%. Based on these results, Actinomucor elegans peptidases were employed to treat the hydrolysates for 3h and 6h, and 1%, 2% β-cyclodextrin (β-CD) were also used to embed hydrolysates to remove bitterness. The results showed that 1% of β-CD treatment can effectively remove bitterness and obtain the highest preservation of the ACE inhibitory activity.
作者 罗贤慧 李理
出处 《中国酿造》 CAS 2012年第10期120-123,共4页 China Brewing
基金 广东省科技攻关项目(2011B020310004)
关键词 高温豆粕 Alcalase2.4L ACE抑制活性 毛霉蛋白酶 Β-CD 脱苦 high-temperature soybean meal Alcalase 2.4L ACE inhibitory activity Actinomucor elegans peptidases β-cyclodextrin bitterness removal
  • 相关文献

参考文献24

  • 1种冠峰,相有章.中国高血压病流行病学及影响因素研究进展[J].中国公共卫生,2010,26(3):301-302. 被引量:164
  • 2SENTANDREU MA, TOLDRA F. Evaluation of ACE inhibitory activity of dipeptides generated bythe action of porcine muscle dipeptidyl peptidases[J]. Food Chem, 2009, 102:511-515.
  • 3MUGURUMA M, AHHMED AM, KATAYAMA K, et al. Identification of pro-drug type ACE inhibitory peptide source from porcine myosin B: Evaluation of its antihypertensive effects in vivo[J]. Food Chem, 2009, 5 (14) : 516-522.
  • 4FERREIRA SH, ROCHA SM. Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothropsjaramca venom[J]. Experlentia, 1965,21 (6) : 347-349.
  • 5ODENTTI MA, WILLIAMS NJ, SABO EF, et al. Angiotensin converting enzyme inhibitors from the venom of Bothropsjararaca. Isolation, elucidation of structure and synthesis[J]. Biochemistry, 1971, 10 (22) : 4033- 4038.
  • 6MA YL, CHENG YQ, YIN L J, et al. Effects of processing and NaCl on angiotensin 1-converting enzyme inhibitory activity and γ-aminobutyric acid content during sufu manufacturing[J]. Food Biopr Technol, 2012, 12: 0852-0854.
  • 7KIM JM, WHANG JH, SUH HJ. Enhancement of angiotensin I converting enzyme inhibitory activityand improvement of the emulsifying and foaming propertiesof com gluten hydrolysate using ultrafiltration mem- brane[J]. Eur Food Res Technol, 2004, 218: 133-138.
  • 8QUIST EE, PHILLIPS RD, SAALIA FK. Angiotensin converting enzyme inhibitory activity of proteolyticdigests of peanut (Arachis hypogaea L.) flour[J]. Food Sci Teehnol, 2009,42: 694-699.
  • 9NAKAJIMA K, YOSHIE-STARK Y, OGUSHI M. Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates[J]. Food Chem, 2009, 114: 844-851.
  • 10MAHMOODANI F, GHASSEM M, BABJI AS, et al. ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate[J]. J Food Sei Teehnol, 2012, 12: 742-749.

二级参考文献136

共引文献249

同被引文献73

引证文献6

二级引证文献34

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部