食品研究与开发
食品研究與開髮
식품연구여개발
FOOD RESEARCH AND CEVELOPMENT
2015年
6期
1-5
,共5页
田斌强%邓乾春%黄娟%谢笔钧
田斌彊%鄧乾春%黃娟%謝筆鈞
전빈강%산건춘%황연%사필균
燕麦%分离蛋白%疏水性%ANS%起泡性
燕麥%分離蛋白%疏水性%ANS%起泡性
연맥%분리단백%소수성%ANS%기포성
oat%protein isolates%surface hydrophobicity%ANS%foaming ablity
采用碱提酸沉法从脱脂燕麦粉中提取得到了蛋白含量为93.01%的分离蛋白(OPI),分析其氨基酸组成,并用ANS荧光探针法研究pH、NaCl、蔗糖、CaCl2、AlCl3和尿素对燕麦分离蛋白疏水性和起泡性的影响。结果表明,OPI氨基酸组成接近FAO/WHO理想模式,pH对燕麦分离蛋白疏水性的影响最大,pH 2时疏水性最强,且酸性环境下的疏水性远远超过碱性环境。不同盐离子对蛋白疏水性的影响程度和趋势不一样,随AlCl3和尿素浓度增加,OPI疏水性减弱;而CaCl2和蔗糖浓度升高时蛋白疏水性增强。NaCl在低浓度(<0.6 mol/L)时蛋白疏水性减弱,高浓度时蛋白疏水性增强。不同因素对OPI起泡性也具有较大的影响,其变化趋势与疏水性较为一致。另外,蔗糖的加入可提高OPI的起泡稳定性,而加入NaCl对其有所降低。
採用堿提痠沉法從脫脂燕麥粉中提取得到瞭蛋白含量為93.01%的分離蛋白(OPI),分析其氨基痠組成,併用ANS熒光探針法研究pH、NaCl、蔗糖、CaCl2、AlCl3和尿素對燕麥分離蛋白疏水性和起泡性的影響。結果錶明,OPI氨基痠組成接近FAO/WHO理想模式,pH對燕麥分離蛋白疏水性的影響最大,pH 2時疏水性最彊,且痠性環境下的疏水性遠遠超過堿性環境。不同鹽離子對蛋白疏水性的影響程度和趨勢不一樣,隨AlCl3和尿素濃度增加,OPI疏水性減弱;而CaCl2和蔗糖濃度升高時蛋白疏水性增彊。NaCl在低濃度(<0.6 mol/L)時蛋白疏水性減弱,高濃度時蛋白疏水性增彊。不同因素對OPI起泡性也具有較大的影響,其變化趨勢與疏水性較為一緻。另外,蔗糖的加入可提高OPI的起泡穩定性,而加入NaCl對其有所降低。
채용감제산침법종탈지연맥분중제취득도료단백함량위93.01%적분리단백(OPI),분석기안기산조성,병용ANS형광탐침법연구pH、NaCl、자당、CaCl2、AlCl3화뇨소대연맥분리단백소수성화기포성적영향。결과표명,OPI안기산조성접근FAO/WHO이상모식,pH대연맥분리단백소수성적영향최대,pH 2시소수성최강,차산성배경하적소수성원원초과감성배경。불동염리자대단백소수성적영향정도화추세불일양,수AlCl3화뇨소농도증가,OPI소수성감약;이CaCl2화자당농도승고시단백소수성증강。NaCl재저농도(<0.6 mol/L)시단백소수성감약,고농도시단백소수성증강。불동인소대OPI기포성야구유교대적영향,기변화추세여소수성교위일치。령외,자당적가입가제고OPI적기포은정성,이가입NaCl대기유소강저。
Oat protein isolates (OPI) were prepared by alkali extraction and isoelectric precipitation from defatted oat groats. OPI contains 93.01%protein. The amino acid composition of the isolates was analyzed , and found that OPI has more hydrophobic amino acids than soy protein isolates and the amino acids composition of OPI is close to the ideal model recommended by FAO/WHO. The hydrophobicity and the isolates were measured using ANS fluorescent probe method at various pH and different concentration solution with NaCl, sucrose, CaCl2, AlCl3 and urea. The foaming ability of OPI was investigated at the same condition. The results showed that pH had the highest influence on the surface hydrophobicity of OPI and the hydrophobicity reaches its peak at pH2;the hydrophobicity of OPI at acid pH was much stronger than that at alkali pH. The trend of effect of different salts on protein hydrophobicity was not same. With AlCl3 and urea concentration increased, the OPI hydrophobicity decreased, but CaCl2 and sucrose was on the contrary. The hydrophobicity decreased in NaCl solution with low concentrations (< 0.6 mol/L) while hydrophobicity enhanced with concentration rising. Different factors had great influence on OPI foaming , the trend was consistent with the hydrophobic. In addition, the addition of sucrose can improve foaming stability of OPI, and the accession to the NaCl reduced it.