浙江农业学报
浙江農業學報
절강농업학보
ACTA AGRICULTURAE ZHEJIANGENSIS
2014年
4期
976-980
,共5页
黄孢原毛平革菌%茶皂素脱色酶%酶学性质
黃孢原毛平革菌%茶皂素脫色酶%酶學性質
황포원모평혁균%다조소탈색매%매학성질
Phanerochaete chrysosporium%tea saponin decoloring enzyme%enzyme properties
对黄孢原毛平革菌( Phanerochaete chrysosporium) TS-07发酵液中的茶皂素脱色酶进行粗分离,并对其酶学性质进行了研究。结果表明:用硫酸铵沉降法所得粗酶粉的酶活力高达52971 U· g-1;该酶的最适反应温度为40℃,最适作用pH值为4.5;该酶在常温下具有良好的热稳定性,在pH值3.0~7.5环境下都比较稳定;Fe3+、Ca2+和Ni2+对酶活影响不大,Hg2+能强烈抑制茶皂素脱色酶的活性;10%( V/V)有机溶剂丙酮、异丙醇、乙醇和乙腈能保留茶皂素脱色酶大部分的活力;反应体系中H2 O2达到5%,茶皂素脱色酶仍能保持较高的活力;而在反应底物不存在的情况下,茶皂素脱色酶与0.25%的H2 O2保温1 h后,酶活残余量仍能达到80%以上。
對黃孢原毛平革菌( Phanerochaete chrysosporium) TS-07髮酵液中的茶皂素脫色酶進行粗分離,併對其酶學性質進行瞭研究。結果錶明:用硫痠銨沉降法所得粗酶粉的酶活力高達52971 U· g-1;該酶的最適反應溫度為40℃,最適作用pH值為4.5;該酶在常溫下具有良好的熱穩定性,在pH值3.0~7.5環境下都比較穩定;Fe3+、Ca2+和Ni2+對酶活影響不大,Hg2+能彊烈抑製茶皂素脫色酶的活性;10%( V/V)有機溶劑丙酮、異丙醇、乙醇和乙腈能保留茶皂素脫色酶大部分的活力;反應體繫中H2 O2達到5%,茶皂素脫色酶仍能保持較高的活力;而在反應底物不存在的情況下,茶皂素脫色酶與0.25%的H2 O2保溫1 h後,酶活殘餘量仍能達到80%以上。
대황포원모평혁균( Phanerochaete chrysosporium) TS-07발효액중적다조소탈색매진행조분리,병대기매학성질진행료연구。결과표명:용류산안침강법소득조매분적매활력고체52971 U· g-1;해매적최괄반응온도위40℃,최괄작용pH치위4.5;해매재상온하구유량호적열은정성,재pH치3.0~7.5배경하도비교은정;Fe3+、Ca2+화Ni2+대매활영향불대,Hg2+능강렬억제다조소탈색매적활성;10%( V/V)유궤용제병동、이병순、을순화을정능보류다조소탈색매대부분적활력;반응체계중H2 O2체도5%,다조소탈색매잉능보지교고적활력;이재반응저물불존재적정황하,다조소탈색매여0.25%적H2 O2보온1 h후,매활잔여량잉능체도80%이상。
A tea saponin decoloring enzyme ( TSDE) was separated from Phanerochaete chrysosporium TS-07 by using ammonium sulfate precipitation .The separated TSDE activity was 52 971 U· g-1 .The effect of pH value on TSDE activity and stability was examined at pH values ranging from 3.0 to 10.0 .TSDE was completely stable in a wide pH range (3.0-7.5) and presented an optimum pH value of 4.5.The optimum temperature for TSDE was 40℃and the enzyme was stable at room temperature .It was also found that TSDE was strongly inhibited by Hg 2+, while Fe3+, Ca2+and Ni2+did not cause any alteration in the activity .TSDE was also resistant to presence of up to 5%H2 O2 , but it was inhibited in presence of 10% H2 O2 .The TSDE showed a high percentage of activity in reaction mixtures containing 10% ( V/V ) of different organic solvents ( acetone , isopropanol , ethanol and acetonitrile).The susceptibility of TSDE to inactivation by H2O2 in absence of substrate was also studied and it was found that the enzyme was very stable in presence of up to 0.25%H2 O2 .