The Emulsifying Property of Enzyme Hydrolysates of Monostroma nitidum

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Project title

Code/計畫編號

NSC83-0406-E019-004

Translated Name/計畫中文名

海菜酵素水解物的乳化特性

Project Coordinator/計畫主持人

Jenn-Shou Tsai

Funding Organization/主管機關

National Science and Technology Council

Department/Unit

Department of Food Science

Website

https://www.grb.gov.tw/search/planDetail?id=112298

Year

1994

Start date/計畫起

01-02-1994

Expected Completion/計畫迄

01-01-1995

Bugetid/研究經費

267千元

ResearchField/研究領域

食品科技(農)

海菜(Monostroma nitidum)經不同抽出方法及酵素處理,探討海菜酵素水解物之凍結乾燥粉末的萃取率及乳化特性。經Cellulase R-10與Macerozyme R-10混合處理3小時後,其萃取率可由未處理者的18.0增至64.9%。海菜酵素水解物之乳化活性隨水解時間的增加而降低,而以Macerozyme R-10處理者最明顯。由膠體層析圖顯示,經水解後低分子量部分的醣量會增加。海菜以Cellulase R-10處理以萃取其熱水可溶的酵素水解物,經噴霧乾燥製成粉末後,其中多醣類約50.0%、蛋白質約6.0%。隨著海菜酵素水解物溶液濃度的增加(0.1-3.0%,w/v),其乳化活性與乳化安定性分別由7.6與5.0%增至54.5與49.0%,但各濃度下仍有油層產生。在不同pH值下,其溶液之黏度、乳化活性、乳化安定性及乳化物之界達電位以pH3.0>pH5.0>pH7.0。利用超過濾法將海菜酵素水解物劃分成1,000kd以上、10至1,000kd與10kd以下三部分,其乳化活性分別為57.0、50.0與2.0%,乳化安定性分別為51.0、48.5與1.0%。海菜酵素水解物經乾熱(60.degree.C,RH65%)反應之結合物,其乳化活性與乳化安定性由51.5與48.0%增至57.6與50.0%,表面疏水性值由44.5增至156.2Se/mg/ml,膠體層析圖中蛋白質位於高/低分子量區域的面積比亦由0.251增至0.343。而添加牛血清蛋白質、酪蛋白鈉與分離大豆蛋白質行乾熱反應者,其結合物的乳化活性分別增至76.4、79.7與83.1%,乳化安定性亦分別增至74.9、75.0與80.8%,而蛋白質位於高/低分子量區域面積比分別增至為0.286、0.334與0.443。海菜酵素水解物之乙醇沈澱物於1%(w/v)的濃度下,乳化活性與乳化安定性分別增至69.0及62.0%,且乳化物無油層產生。而未沈澱物則分別降為42.5與40.0%,且油層由1.0與2.0%分別增至7.5與10.0%。由膠體層析圖顯示,乙醇沈澱物中位於高分子量部分之蛋白質與多醣類的量會增加。隨著乙醇沈澱物濃度的增加(0-20mg/ml),其溶液的表面張力下降至54.9dynes/cm,CMC值為3.9mg/ml。乙醇沈澱物的乳化能力隨濃度(0.1-2.0%,w/v)的增加,乳化活性與乳化安定性可提高至76.9及70.0%。以NaCl調整離子強度(0-0.2)時,乙醇沈澱物溶液黏度由37.1降至7.6cps;乳化活性與乳化安定性分別由69.0與62.0%降至50.0與48.0%,乳化物之界達電位由63.9降至28.2(-mV)。以緩衝液調整乙醇沈澱物溶液之pH值,其溶液的黏度、乳化活性、乳化安定性及乳化物的界達電位依序為pH3.0>pH5.0>pH7.0。乙醇沈澱物以酵素Pronase E水解3小時後,其乳化活性與乳化安定性分別下降至61.0與56.5%,且皆有2%油層產生,而溶液的黏度與乳化物的界達電位則分別下降至25.2cps與49.2(-mV)。利用膠體層析圖分析顯示,乙醇沈澱物經水解後蛋白質位於高/低分子量部分的面積比由5.13下降至2.95。 The extraction yield and emulsifying properties of freeze-dried enzymatic hydrolysate from Monostroma nitidum prepared by various process methods and enzymatic hydrolysis were investigated. The extraction yield increased from 18.0% using no hydrolysis to 64.9% by using a combination of cellulase R-10 (E/S=3.0%) and Macerozyme R-10 (E/S=3.0%) for 3hr. The emulsifying activity of enzymatic hydrolysate from Monostroma nitidum decreased with hydrolysis time. The Macerozyme R-10 hydrolysis resulted in obvious decrease. Increases of carbohydrate content in the low molecular weight area with enzymatic hydrolysis were found by gel permeation chromatography. Monostroma nitidum treated with cellulase R-10 to extract the hot-water soluble enzymatic hydrolysate and spray-dried resulted in 50.0% of polysaccharide and 6.0% of protein. Increasing the hydrolysate concentration of the solution (0-3.0%), the emulsifying activity and emulsion stability increased from 7.6 and 5.0% to 54.5 and 49.0%, respectively, and oil was separated from the emulsion at these concentrations. The solution apparent viscosity and the emulsifying activity, emulsion stability and zeta potential of emulsion at different pH's were all shown to follow the order of pH3.0>pH5.0>pH7.0. By ultrafiltration, the hydrolysate was fractionated into three fractions based on molecular weight: higher than 1,000kd, 10-1,000kd and lower than 10kd. The emulsifying activity was 57.0, 50.0 and 2.0%, and emulsion stability was 51.0, 48.5 and 1.0%, respectively. By dry-heating at 60.degree.C, RH65%, the emulsifying activity and emulsion stability of the conjugates of the hydrolysate increased from 51.5 and 48.0% to 57.6 and 50.0%, respectively. The surface hydrophobicity increased from 44.5 to 156.2Se/mg/ml. The ratio of protein high/low molecular weight peak area increased from 0.251 to 0.343. Conjugates with bovine serum albumin (BSA), sodium caseinate (SC) and soy protein isolate (SPI) prepared by dry-heating increased the emulsifying activity to 76.4, 79.7 and 83.1%; increased the emulsion stability to 74.9, 75.0 and 80.8%; and increased the ratio of protein high/low molecular weight peak area to 0.286, 0.334 and 0.443, respectively. When using ethanolic precipitation both emulsifying activity and emulsion stability increased to 69.0 and 62.0%, respectively, and oil was not separated from emulsion when the concentration was at 1% (w/v). However, the emulsifying activity and emulsion stability of the dried supernate decreased to 42.5 and 40.0%, respectively, and the oil layer increased from 1.0 and 2.0% to 7.5 and 10.0%, respectively, at the same concentration. Increased protein and carbohydrate content was found by gel permeation chromatography in the high molecular weight area of the ethanolic precipitate. Increasing the ethanolic precipitate concentration of solution (0-20mg/ml) led to a reduction of surface tension to 54.9 dyne/cm, and the critical micelle concentration was 3.9mg/ml. The emulsifying activity and emulsion stability increased to 76.9 and 70.0%, respectively. When ionic strength was increased to 0.2 by adding NaCl, the solution apparent viscosity decreased from 37.1 to 7.6cps; the emulsifying activity and emulsion stability decreased 69.0 and 62.0% to 50.0 and 48.0%, respectively; and the zeta potential of emulsion decreased from 63.9 to 28.2 (-mV). The solution apparent viscosity and emulsifying activity, emulsion stability and zeta potential of emulsion at different pH's which were controlled by buffer were all shown to follow the order of pH3.0>pH5.0>pH7.0. Using pronase E to hydrolyze the ethanolic precipitate for 3hr, the emulsifying activity and emulsion stability decreased to 61.0 and 56.5%, respectively, and both had 2% oil separated from emulsion, and the solution apparent viscosity and zeta potential of emulsion decreased to 25.2cps and 49

Keyword(s)

海菜
乳化
酵素水解
Monostroma nitidum
Emulsification
Enzyme hydrolyzation

DSpace CRIS

The Emulsifying Property of Enzyme Hydrolysates of Monostroma nitidum

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