可控酶解从海洋鱼蛋白中制备生物活性肽的研究

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1、华南理工大学博士学位论文可控酶解从海洋鱼蛋白中制备生物活性肽的研究姓名：林伟锋申请学位级别：博士专业：食品科学指导教师：彭志英;赵谋明20030701华素壤工夫学工学簿±学建论文鼠的游泳时闻呈正相关关系，低分子爨组分的对延长小自鼠游泳时阅的作用比商分子量组分的效聚更显蔫；活髋肽能鼗著提高小自鼠煎肝糖藤贮备麓，活径肤的剂攫与小臼鼠疲劳时的肝糖原含量呈正相关关系；低分子量组分对提升小自鼠肝糖藤贮备麓的作掰眈高分子蟹缀分的作用显著，低分子量活住肷组分其有撼著的促进机体物质代谢，提黼其肝糖原的贮备量的作用；活性肽熊降低疲劳小

2、臼鼠体内酶盔藤豢氮静含量，潇往虢的灌霉裁璧与夺盘鼠酶疲劳时的血尿素氮含蚤有负相关关系，低分子量组分对降低血尿素氮含量的效果比高分子量组分的显蔫。低分予量活性获稳离分子爨活瞧获都其霄抗疲劳活性，并涟羞灌胃裁蘩静提离焉增强，低分子量活性肽比商分子量活性肽舆有更高的抗疲劳活性。关键词：生物活1攮肽；可控酶解；动力学模型；分离纯化；抗疲劳活性娃AbstractInthispaper,studiesonpreparationofbiologicallyactivepeptidesbyuseofcontrolled-enzyma

3、tichydrolysisofsardineprotein，ultrafiltrationandion-exchange，andanti—fatigueactionwerecarriedout．Studiesofcontrolled-enzymatichydrolysisweremainlyOntheeffectofpH，hydrolyzedtime，dosageandvarietiesofproteases，concentrationandvarietiesofsubstrate，hydrolyzedtempera

4、tureandstirringmodeonhydrolyzedresultanddistributionofmolecularweight．Experimentalresultisasfollows．BasisonchangeofpHhaslittleeffectonrecoveryratioofpeptidesanddistributionofmolecularweight，thereisnoneedtoaddalkalitokeeppHconstantduringhydrolysis．Thecourseofhyd

5、rolysismaybedividedintothreestages．Theyarequickraise-stage，slowincrement-stageandplateau—stage，andthemainreasontothatisthedecreaseofconcentrationofsubstrate。AshydrotyzedtimegoesOn，peptidechainlengthofhydrolysateswilldecrease，thecontentofhighmolecularweightwilld

6、ecline，andoncontrary,thecontentoftowmolecularweightwillrise．ThebesthydrolyzedresultisTrypsin，andthenisAIcalaseandProtamex，theworstisNeutrase．Theoptimumdosagesoffourkindsofproteasesareall2000U／g～3000U／g．Toohighbeginningsubstrateconcentrationwilldecreasetheveloci

7、tyofhydrolyzedreaction．Theoptimumbeginningsubstrateconcentrationis7．5％。Thehydrotyzedres}ultofsardineisbetterthanofnemipterus．TheoptimumhydrolyzedtemperatureofTrypsinandAlcalaseisabout55℃。theoptimumoneofProtamexandNeutraseis50"Caround，andtheoptimumtemperatureofa

8、uto-hydrolysisis45"C．Thehydrolyzedresultbycontinuousstirismorebetter．Thebeginningconcentrationandthevarietyofproteaseandsubstratewillhavenotableeffectonrelationshipbetweende