Changes in Molecular Subunit Composition and Allergenicity of Soybean Proteins during Enzymatic Hydrolysis

doi:10.7506/spkx1002-6630-201309054

Abstract

Abstract:

This study was to investigate the effects of enzymatic hydrolysis by three enzymes (alcalase, papain and trypsin)
on molecular subunit composition and allergenicity of soybean meal proteins. The molecular subunits of soybean proteins
in soluble hydrolysate and insoluble residue were analyzed with SDS-PAGE. The contents of allergenic proteins in the two
hydrolysates were measured by enzyme-linked immunosorbent assay (ELISA). The results showed that the major α’, α,
β-subunits of β-conglycinin (7S) and the acidic polypeptide of glycinin (11S) in the two hydrolysates almost disappeared
after hydrolysis for 10 min by alcalase or papain. The content of allergenic proteins was reduced from 195.90 mg/g soybean
meal to 90.50 mg/g (alcalase) and 94.30 mg/g (papain) total hydrolysates, respectively, over half of allergenicity in soybean
meal being eliminated. After 120 min hydrolysis by alcalase and papain, the rate of eliminated allergenicity was 75.70% and
61.40% respectively. Nevertheless the effect of trypsin on the molecular subunits composition and allergenic proteins was
not evident compared to alcalase and papain. The results above indicated that enzymatic hydrolysis by alcalase or papain
could efficiently reduce the allergenicity of soybean meal.

Key words: soybean meal, enzymatic hydrolysis, protein subunit, allergenicity, ELISA

CLC Number:

TS201.6

WANG Zhang-cun，LI Le-jing，YUAN Dao-qiang，CUI Sheng-wen，ZHAO Xue-wei，WANG Ji-zhong，HU Jin-qiang. Changes in Molecular Subunit Composition and Allergenicity of Soybean Proteins during Enzymatic Hydrolysis[J]. FOOD SCIENCE, 2013, 34(9): 267-270.

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