Biopolymers Produced by Cross-linking Soybean 11S Globulin with Whey Proteins using Transglutaminase

Authors

  • M. YILDIRIM,

    1. Authors Yildirim and Hettiarachchy are with the Dept. of Food Science, Univ. of Arkansas, 272 Young Ave., Fayetteville, AR 72704. Direct inquiries to Dr. N.S. Hettiarachchy.
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  • N.S. HETTIARACHCHY

    1. Authors Yildirim and Hettiarachchy are with the Dept. of Food Science, Univ. of Arkansas, 272 Young Ave., Fayetteville, AR 72704. Direct inquiries to Dr. N.S. Hettiarachchy.
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  • The skillful technical assistance of Dr. U. Kalapathy is gratefully acknowledged. We thank Dr. M.R. Coleman, Department of Chemical Engineering, for use of the DSC equipment. Mr. M. Yildirim was the recipient of a Turkish Government Fellowship. Funds provided by the United Soybean Board for supplies are appreciated.

ABSTRACT

Heterogeneity of biopolymers was determined by cross-linking acetylated-11S acidic subunits (Ac-11S) of soy protein with α-lactalbumin and β-lactoglobulin. The extent of polymerization was determined by electrophoresis and HPLC. Differential scanning calorimetry (DSC) was used to determine thermal properties of starting proteins and biopolymers. HPLC data demonstrated the absence of biopolymers from Ac-11S, acetylated α-lactalbumin and acetylated β-lactoglobulin when each was incubated separately with transglutaminase (TG). However, Ac-11S formed biopolymers with α-lactalbumin and β-lactoglobulin when TG was added. TG catalyzed the formation of heterologous and homologous biopolymers from whey protein isolate (WPI) and soybean 11S globulin (11S). Cross-linking WPI and 11S provided biopolymers with improved heat stability which may be useful to provide functionality to food products.

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